Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta

L Zhao; J B Helms; B Brügger; C Harter; B Martoglio; R Graf; J Brunner; F T Wieland

Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta

L Zhao, J B Helms, B Brügger, C Harter, B Martoglio, R Graf, J Brunner, F T Wieland

Heidelberg University

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

A site-directed photocrosslink approach was used to elucidate components that interact directly with ADP- ribosylation factor (ARF)-GTP during coat assembly. Two ARF mutants were generated that contain a photolabile amino acid at positions distant to each other within the ARF molecule. Here we show that one of the two positions specifically interacts with coatomer subunit beta both on Golgi membranes and in isolated coat protein complex type I (COPI)-coated vesicles. Thus, a direct and GTP-dependent interaction of coatomer via beta-coat protein complex (COP) with ARF is involved in the coating of COPI-coated vesicles. These data implicate a bivalent interaction of the complex with the donor membrane during vesicle formation.

Original language	English
Pages (from-to)	4418-23
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	94
Issue number	9
Publication status	Published - 29 Apr 1997

Keywords

ADP-Ribosylation Factors
Affinity Labels
Azirines
Biological Transport
Coated Vesicles
Coatomer Protein
Endoplasmic Reticulum
GTP-Binding Proteins
Guanosine 5'-O-(3-Thiotriphosphate)
Guanosine Triphosphate
Membrane Proteins
Microtubule-Associated Proteins
Mutation
Phenylalanine
Precipitin Tests
Protein Binding
Ultraviolet Rays

Cite this

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title = "Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta",

abstract = "A site-directed photocrosslink approach was used to elucidate components that interact directly with ADP- ribosylation factor (ARF)-GTP during coat assembly. Two ARF mutants were generated that contain a photolabile amino acid at positions distant to each other within the ARF molecule. Here we show that one of the two positions specifically interacts with coatomer subunit beta both on Golgi membranes and in isolated coat protein complex type I (COPI)-coated vesicles. Thus, a direct and GTP-dependent interaction of coatomer via beta-coat protein complex (COP) with ARF is involved in the coating of COPI-coated vesicles. These data implicate a bivalent interaction of the complex with the donor membrane during vesicle formation.",

keywords = "ADP-Ribosylation Factors, Affinity Labels, Azirines, Biological Transport, Coated Vesicles, Coatomer Protein, Endoplasmic Reticulum, GTP-Binding Proteins, Guanosine 5'-O-(3-Thiotriphosphate), Guanosine Triphosphate, Membrane Proteins, Microtubule-Associated Proteins, Mutation, Phenylalanine, Precipitin Tests, Protein Binding, Ultraviolet Rays",

author = "L Zhao and Helms, {J B} and B Br{\"u}gger and C Harter and B Martoglio and R Graf and J Brunner and Wieland, {F T}",

year = "1997",

month = apr,

day = "29",

language = "English",

volume = "94",

pages = "4418--23",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "9",

}

TY - JOUR

T1 - Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta

AU - Zhao, L

AU - Helms, J B

AU - Brügger, B

AU - Harter, C

AU - Martoglio, B

AU - Graf, R

AU - Brunner, J

AU - Wieland, F T

PY - 1997/4/29

Y1 - 1997/4/29

N2 - A site-directed photocrosslink approach was used to elucidate components that interact directly with ADP- ribosylation factor (ARF)-GTP during coat assembly. Two ARF mutants were generated that contain a photolabile amino acid at positions distant to each other within the ARF molecule. Here we show that one of the two positions specifically interacts with coatomer subunit beta both on Golgi membranes and in isolated coat protein complex type I (COPI)-coated vesicles. Thus, a direct and GTP-dependent interaction of coatomer via beta-coat protein complex (COP) with ARF is involved in the coating of COPI-coated vesicles. These data implicate a bivalent interaction of the complex with the donor membrane during vesicle formation.

AB - A site-directed photocrosslink approach was used to elucidate components that interact directly with ADP- ribosylation factor (ARF)-GTP during coat assembly. Two ARF mutants were generated that contain a photolabile amino acid at positions distant to each other within the ARF molecule. Here we show that one of the two positions specifically interacts with coatomer subunit beta both on Golgi membranes and in isolated coat protein complex type I (COPI)-coated vesicles. Thus, a direct and GTP-dependent interaction of coatomer via beta-coat protein complex (COP) with ARF is involved in the coating of COPI-coated vesicles. These data implicate a bivalent interaction of the complex with the donor membrane during vesicle formation.

KW - ADP-Ribosylation Factors

KW - Affinity Labels

KW - Azirines

KW - Biological Transport

KW - Coated Vesicles

KW - Coatomer Protein

KW - Endoplasmic Reticulum

KW - GTP-Binding Proteins

KW - Guanosine 5'-O-(3-Thiotriphosphate)

KW - Guanosine Triphosphate

KW - Membrane Proteins

KW - Microtubule-Associated Proteins

KW - Mutation

KW - Phenylalanine

KW - Precipitin Tests

KW - Protein Binding

KW - Ultraviolet Rays

M3 - Article

C2 - 9114004

SN - 0027-8424

VL - 94

SP - 4418

EP - 4423

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 9

ER -

Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta

Abstract

Keywords

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