Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule.

Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin...
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Gespeichert in:

Autor*in:	Krantz, D.E. [verfasserIn] Zipursky, S.L. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	1990

Anmerkung:	© European Molecular Biology Organization 1990

Übergeordnetes Werk:	Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 9(1990), 6 vom: 01. Juni, Seite 1969-1977
Übergeordnetes Werk:	volume:9 ; year:1990 ; number:6 ; day:01 ; month:06 ; pages:1969-1977

Links:	Volltext

DOI / URN:	10.1002/j.1460-2075.1990.tb08325.x

Katalog-ID:	SPR057582254

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520			\|a Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules.
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allfields	10.1002/j.1460-2075.1990.tb08325.x doi (DE-627)SPR057582254 (SPR)j.1460-2075.1990.tb08325.x-e DE-627 ger DE-627 rakwb eng Krantz, D.E. verfasserin aut Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule. 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1990 Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. Zipursky, S.L. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 9(1990), 6 vom: 01. Juni, Seite 1969-1977 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:9 year:1990 number:6 day:01 month:06 pages:1969-1977 https://dx.doi.org/10.1002/j.1460-2075.1990.tb08325.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 1990 6 01 06 1969-1977
spelling	10.1002/j.1460-2075.1990.tb08325.x doi (DE-627)SPR057582254 (SPR)j.1460-2075.1990.tb08325.x-e DE-627 ger DE-627 rakwb eng Krantz, D.E. verfasserin aut Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule. 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1990 Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. Zipursky, S.L. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 9(1990), 6 vom: 01. Juni, Seite 1969-1977 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:9 year:1990 number:6 day:01 month:06 pages:1969-1977 https://dx.doi.org/10.1002/j.1460-2075.1990.tb08325.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 1990 6 01 06 1969-1977
allfields_unstemmed	10.1002/j.1460-2075.1990.tb08325.x doi (DE-627)SPR057582254 (SPR)j.1460-2075.1990.tb08325.x-e DE-627 ger DE-627 rakwb eng Krantz, D.E. verfasserin aut Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule. 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1990 Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. Zipursky, S.L. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 9(1990), 6 vom: 01. Juni, Seite 1969-1977 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:9 year:1990 number:6 day:01 month:06 pages:1969-1977 https://dx.doi.org/10.1002/j.1460-2075.1990.tb08325.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 1990 6 01 06 1969-1977
allfieldsGer	10.1002/j.1460-2075.1990.tb08325.x doi (DE-627)SPR057582254 (SPR)j.1460-2075.1990.tb08325.x-e DE-627 ger DE-627 rakwb eng Krantz, D.E. verfasserin aut Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule. 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1990 Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. Zipursky, S.L. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 9(1990), 6 vom: 01. Juni, Seite 1969-1977 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:9 year:1990 number:6 day:01 month:06 pages:1969-1977 https://dx.doi.org/10.1002/j.1460-2075.1990.tb08325.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 1990 6 01 06 1969-1977
allfieldsSound	10.1002/j.1460-2075.1990.tb08325.x doi (DE-627)SPR057582254 (SPR)j.1460-2075.1990.tb08325.x-e DE-627 ger DE-627 rakwb eng Krantz, D.E. verfasserin aut Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule. 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1990 Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. Zipursky, S.L. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 9(1990), 6 vom: 01. Juni, Seite 1969-1977 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:9 year:1990 number:6 day:01 month:06 pages:1969-1977 https://dx.doi.org/10.1002/j.1460-2075.1990.tb08325.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 1990 6 01 06 1969-1977
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author	Krantz, D.E.
spellingShingle	Krantz, D.E. Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule.
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topic_title	Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule
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title	Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule.
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title_full	Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule
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title_sort	drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule
title_auth	Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule.
abstract	Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. © European Molecular Biology Organization 1990
abstractGer	Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. © European Molecular Biology Organization 1990
abstract_unstemmed	Abstract Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine‐rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non‐self‐adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non‐expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell‐type‐specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol. We propose that chaoptin and several other members of the leucine‐rich repeat family of proteins define a new class of cell adhesion molecules. © European Molecular Biology Organization 1990
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container_issue	6
title_short	Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule.
url	https://dx.doi.org/10.1002/j.1460-2075.1990.tb08325.x
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