Structure and binding of the C-terminal segment of R9AP to lipid monolayers
Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Bernier, Sarah C [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Schlagwörter: |
Adaptor Proteins, Signal Transducing - chemistry Membrane Proteins - metabolism Adaptor Proteins, Signal Transducing - metabolism |
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| Systematik: |
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| Übergeordnetes Werk: |
Enthalten in: Langmuir - Washington, DC : ACS Publ., 1985, 31(2015), 6, Seite 1967 |
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| Übergeordnetes Werk: |
volume:31 ; year:2015 ; number:6 ; pages:1967 |
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| 520 | |a Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. | ||
| 650 | 4 | |a Adaptor Proteins, Signal Transducing - chemistry | |
| 650 | 4 | |a Membrane Lipids - metabolism | |
| 650 | 4 | |a Peptide Fragments - chemistry | |
| 650 | 4 | |a Membrane Proteins - chemistry | |
| 650 | 4 | |a Membrane Proteins - metabolism | |
| 650 | 4 | |a Membrane Lipids - chemistry | |
| 650 | 4 | |a Adaptor Proteins, Signal Transducing - metabolism | |
| 650 | 4 | |a Peptide Fragments - metabolism | |
| 650 | 4 | |a Phospholipids - metabolism | |
| 700 | 1 | |a Horchani, Habib |4 oth | |
| 700 | 1 | |a Salesse, Christian |4 oth | |
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PQ20160617 (DE-627)OLC1957078901 (DE-599)GBVOLC1957078901 (PRQ)p477-a6ae8975db4028cfb7042972a8e584d151de2a213839f75f0cabbc7b0d44ec200 (KEY)0138429520150000031000601967structureandbindingofthecterminalsegmentofr9aptoli DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Bernier, Sarah C verfasserin aut Structure and binding of the C-terminal segment of R9AP to lipid monolayers 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. Adaptor Proteins, Signal Transducing - chemistry Membrane Lipids - metabolism Peptide Fragments - chemistry Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Lipids - chemistry Adaptor Proteins, Signal Transducing - metabolism Peptide Fragments - metabolism Phospholipids - metabolism Horchani, Habib oth Salesse, Christian oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 6, Seite 1967 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:6 pages:1967 http://www.ncbi.nlm.nih.gov/pubmed/25614992 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 6 1967 |
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PQ20160617 (DE-627)OLC1957078901 (DE-599)GBVOLC1957078901 (PRQ)p477-a6ae8975db4028cfb7042972a8e584d151de2a213839f75f0cabbc7b0d44ec200 (KEY)0138429520150000031000601967structureandbindingofthecterminalsegmentofr9aptoli DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Bernier, Sarah C verfasserin aut Structure and binding of the C-terminal segment of R9AP to lipid monolayers 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. Adaptor Proteins, Signal Transducing - chemistry Membrane Lipids - metabolism Peptide Fragments - chemistry Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Lipids - chemistry Adaptor Proteins, Signal Transducing - metabolism Peptide Fragments - metabolism Phospholipids - metabolism Horchani, Habib oth Salesse, Christian oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 6, Seite 1967 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:6 pages:1967 http://www.ncbi.nlm.nih.gov/pubmed/25614992 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 6 1967 |
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PQ20160617 (DE-627)OLC1957078901 (DE-599)GBVOLC1957078901 (PRQ)p477-a6ae8975db4028cfb7042972a8e584d151de2a213839f75f0cabbc7b0d44ec200 (KEY)0138429520150000031000601967structureandbindingofthecterminalsegmentofr9aptoli DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Bernier, Sarah C verfasserin aut Structure and binding of the C-terminal segment of R9AP to lipid monolayers 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. Adaptor Proteins, Signal Transducing - chemistry Membrane Lipids - metabolism Peptide Fragments - chemistry Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Lipids - chemistry Adaptor Proteins, Signal Transducing - metabolism Peptide Fragments - metabolism Phospholipids - metabolism Horchani, Habib oth Salesse, Christian oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 6, Seite 1967 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:6 pages:1967 http://www.ncbi.nlm.nih.gov/pubmed/25614992 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 6 1967 |
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PQ20160617 (DE-627)OLC1957078901 (DE-599)GBVOLC1957078901 (PRQ)p477-a6ae8975db4028cfb7042972a8e584d151de2a213839f75f0cabbc7b0d44ec200 (KEY)0138429520150000031000601967structureandbindingofthecterminalsegmentofr9aptoli DE-627 ger DE-627 rakwb eng 670 540 DE-600 VA 5760 AVZ rvk 35.18 bkl Bernier, Sarah C verfasserin aut Structure and binding of the C-terminal segment of R9AP to lipid monolayers 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. Adaptor Proteins, Signal Transducing - chemistry Membrane Lipids - metabolism Peptide Fragments - chemistry Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Lipids - chemistry Adaptor Proteins, Signal Transducing - metabolism Peptide Fragments - metabolism Phospholipids - metabolism Horchani, Habib oth Salesse, Christian oth Enthalten in Langmuir Washington, DC : ACS Publ., 1985 31(2015), 6, Seite 1967 (DE-627)129170690 (DE-600)50983-8 (DE-576)01445520X 0743-7463 nnns volume:31 year:2015 number:6 pages:1967 http://www.ncbi.nlm.nih.gov/pubmed/25614992 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_2007 VA 5760 35.18 AVZ AR 31 2015 6 1967 |
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Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. 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structure and binding of the c-terminal segment of r9ap to lipid monolayers |
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Structure and binding of the C-terminal segment of R9AP to lipid monolayers |
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Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. |
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Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. |
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Phototransduction cascade takes place in disc membranes of photoreceptor cells. Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound α-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells. PDE6 must then be inactivated to return to the dark state. This is achieved by a protein complex which is presumably anchored to photoreceptor disc membranes by means of the transmembrane C-terminal segment of RGS9-1-Anchor Protein (R9AP). Information on the secondary structure and membrane binding properties of the C-terminal segment of R9AP is not yet available to further support its role in the membrane anchoring of this protein. In the present study, circular dichroism and infrared spectroscopy measurements have allowed us to determine that the C-terminal segment of human and bovine R9AP adopts an α-helical structure in solution. Moreover, this C-terminal segment has shown affinity for most of the phospholipids typical of photoreceptor membranes. In fact, the physical state and the type of phospholipid as well as electrostatic interactions influence the binding of the human and bovine peptides to phospholipid monolayers. In addition, these measurements revealed that the human peptide has a high affinity for saturated phosphocholine, which may suggest a possible localization of R9AP in photoreceptor microdomains. Accordingly, infrared spectroscopy measurements have allowed determining that the C-terminal segment of R9AP adopts an ordered α-helical structure in the presence of saturated phospholipid monolayers. Altogether, these data are consistent with the typical α-helical secondary structure and behavior observed for transmembrane segments and with the proposed role of membrane anchoring of the C-terminal segment of human and bovine R9AP. |
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