Dynamic multiprotein assemblies shape the spatial structure of cell signaling
Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways;...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Nussinov, Ruth [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014transfer abstract |
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| Schlagwörter: |
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| Umfang: |
7 |
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| Übergeordnetes Werk: |
Enthalten in: A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital - Ma, Luping ELSEVIER, 2022, an international review journal, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:116 ; year:2014 ; number:2 ; pages:158-164 ; extent:7 |
| Links: |
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| DOI / URN: |
10.1016/j.pbiomolbio.2014.07.002 |
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ELV018121047 |
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| 520 | |a Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. | ||
| 520 | |a Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. | ||
| 650 | 7 | |a Cell structure |2 Elsevier | |
| 650 | 7 | |a Signal transduction |2 Elsevier | |
| 650 | 7 | |a Signaling modules |2 Elsevier | |
| 650 | 7 | |a Cell organization |2 Elsevier | |
| 650 | 7 | |a Diffusion |2 Elsevier | |
| 650 | 7 | |a Cell signaling |2 Elsevier | |
| 700 | 1 | |a Jang, Hyunbum |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Ma, Luping ELSEVIER |t A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital |d 2022 |d an international review journal |g Amsterdam [u.a.] |w (DE-627)ELV007634501 |
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10.1016/j.pbiomolbio.2014.07.002 doi GBVA2014023000018.pica (DE-627)ELV018121047 (ELSEVIER)S0079-6107(14)00064-9 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Nussinov, Ruth verfasserin aut Dynamic multiprotein assemblies shape the spatial structure of cell signaling 2014transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell structure Elsevier Signal transduction Elsevier Signaling modules Elsevier Cell organization Elsevier Diffusion Elsevier Cell signaling Elsevier Jang, Hyunbum oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:116 year:2014 number:2 pages:158-164 extent:7 https://doi.org/10.1016/j.pbiomolbio.2014.07.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 116 2014 2 158-164 7 045F 570 |
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10.1016/j.pbiomolbio.2014.07.002 doi GBVA2014023000018.pica (DE-627)ELV018121047 (ELSEVIER)S0079-6107(14)00064-9 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Nussinov, Ruth verfasserin aut Dynamic multiprotein assemblies shape the spatial structure of cell signaling 2014transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell structure Elsevier Signal transduction Elsevier Signaling modules Elsevier Cell organization Elsevier Diffusion Elsevier Cell signaling Elsevier Jang, Hyunbum oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:116 year:2014 number:2 pages:158-164 extent:7 https://doi.org/10.1016/j.pbiomolbio.2014.07.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 116 2014 2 158-164 7 045F 570 |
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10.1016/j.pbiomolbio.2014.07.002 doi GBVA2014023000018.pica (DE-627)ELV018121047 (ELSEVIER)S0079-6107(14)00064-9 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Nussinov, Ruth verfasserin aut Dynamic multiprotein assemblies shape the spatial structure of cell signaling 2014transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell structure Elsevier Signal transduction Elsevier Signaling modules Elsevier Cell organization Elsevier Diffusion Elsevier Cell signaling Elsevier Jang, Hyunbum oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:116 year:2014 number:2 pages:158-164 extent:7 https://doi.org/10.1016/j.pbiomolbio.2014.07.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 116 2014 2 158-164 7 045F 570 |
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10.1016/j.pbiomolbio.2014.07.002 doi GBVA2014023000018.pica (DE-627)ELV018121047 (ELSEVIER)S0079-6107(14)00064-9 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Nussinov, Ruth verfasserin aut Dynamic multiprotein assemblies shape the spatial structure of cell signaling 2014transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell structure Elsevier Signal transduction Elsevier Signaling modules Elsevier Cell organization Elsevier Diffusion Elsevier Cell signaling Elsevier Jang, Hyunbum oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:116 year:2014 number:2 pages:158-164 extent:7 https://doi.org/10.1016/j.pbiomolbio.2014.07.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 116 2014 2 158-164 7 045F 570 |
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10.1016/j.pbiomolbio.2014.07.002 doi GBVA2014023000018.pica (DE-627)ELV018121047 (ELSEVIER)S0079-6107(14)00064-9 DE-627 ger DE-627 rakwb eng 570 570 DE-600 690 VZ 56.00 bkl Nussinov, Ruth verfasserin aut Dynamic multiprotein assemblies shape the spatial structure of cell signaling 2014transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. Cell structure Elsevier Signal transduction Elsevier Signaling modules Elsevier Cell organization Elsevier Diffusion Elsevier Cell signaling Elsevier Jang, Hyunbum oth Enthalten in Elsevier Science Ma, Luping ELSEVIER A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital 2022 an international review journal Amsterdam [u.a.] (DE-627)ELV007634501 volume:116 year:2014 number:2 pages:158-164 extent:7 https://doi.org/10.1016/j.pbiomolbio.2014.07.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 56.00 Bauwesen: Allgemeines VZ AR 116 2014 2 158-164 7 045F 570 |
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Enthalten in A multi-zone spatial flow impact factor model for evaluating and layout optimization of infection risk in a Fangcang shelter hospital Amsterdam [u.a.] volume:116 year:2014 number:2 pages:158-164 extent:7 |
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Dynamic multiprotein assemblies shape the spatial structure of cell signaling |
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Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. |
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Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. |
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Cell signaling underlies critical cellular decisions. Coordination, efficiency as well as fail-safe mechanisms are key elements. How the cell ensures that these hallmarks are at play are important questions. Cell signaling is often viewed as taking place through discrete and cross-talking pathways; oftentimes these are modularized to emphasize distinct functions. While simple, convenient and clear, such models largely neglect the spatial structure of cell signaling; they also convey inter-modular (or inter-protein) spatial separation that may not exist. Here our thesis is that cell signaling is shaped by a network of multiprotein assemblies. While pre-organized, the assemblies and network are loose and dynamic. They contain transiently-associated multiprotein complexes which are often mediated by scaffolding proteins. They are also typically anchored in the membrane, and their continuum may span the cell. IQGAP1 scaffolding protein which binds proteins including Raf, calmodulin, Mek, Erk, actin, and tens more, with actin shaping B-cell (and likely other) membrane-anchored nanoclusters and allosterically polymerizing in dynamic cytoskeleton formation, and Raf anchoring in the membrane along with Ras, provides a striking example. The multivalent network of dynamic proteins and lipids, with specific interactions forming and breaking, can be viewed as endowing gel-like properties. Collectively, this reasons that efficient, productive and reliable cell signaling takes place primarily through transient, preorganized and cooperative protein–protein interactions spanning the cell rather than stochastic, diffusion-controlled processes. |
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