Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum

The binding and hydrolysis of guanosine triphosphate (GTP) by the small GTP-binding protein Sar1p is required to form transport vesicles from the endoplasmic reticulum (ER) in Saccharomyces cerevisiae. Experiments revealed that an interaction between Sar1p and the Sec23p subunit of an oligomeric pro...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1993-03, Vol.259 (5100), p.1466-1468
Main Authors: Yoshihisa, T. (University of California, Berkeley, CA), Barlowe, C, Schekman, R
Format: Article
Language:English
Subjects:
Alleles
Antibodies
Biological and medical sciences
Budding
Cell physiology
Circles
Cloning, Molecular
COP-Coated Vesicles
ECUSSONNAGE
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum - ultrastructure
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Fungal Proteins - metabolism
G proteins
Genes, Fungal
GTP-Binding Proteins - genetics
GTP-Binding Proteins - metabolism
GTPase activating proteins
GTPase-activating protein
GTPases
Guanosine triphosphatase
Hydrolysis
INJERTO DE YEMA
Kinetics
Macromolecular Substances
Membrane and intracellular transports
Molecular and cellular biology
Monomeric GTP-Binding Proteins
Monomers
Mutagenesis
NUCLEOTIDE
NUCLEOTIDOS
PROTEINAS
PROTEINE
Proteins - metabolism
RETICULO ENDOPLASMATICO
RETICULUM ENDOPLASMIQUE
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
Spheroplasts - metabolism
Transport vesicles
vesicles
Vesicular Transport Proteins
Yeasts
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Summary:The binding and hydrolysis of guanosine triphosphate (GTP) by the small GTP-binding protein Sar1p is required to form transport vesicles from the endoplasmic reticulum (ER) in Saccharomyces cerevisiae. Experiments revealed that an interaction between Sar1p and the Sec23p subunit of an oligomeric protein is also required for vesicle budding. The isolated Sec23p subunit and the oligomeric complex stimulated guanosine triphosphatase (GTPase) activity of Sar1p 10- to 15-fold but did not activate two other small GTP-binding proteins involved in vesicle traffic (Ypt1p and ARF). Activation of GTPase was inhibited by an antibody to Sec23p but not by an antibody that inhibits the budding activity of the other subunit of the Sec23p complex. Also, activation was thermolabile in pure samples of Sec23p that were isolated from two independent sec23 mutant strains. It appears that Sec23p represents a new class of GTPase-activating protein because its sequence shows no similarity to any known member of this family
ISSN:0036-8075
1095-9203
DOI:10.1126/science.8451644