Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-7-7
pubmed:abstractText
Ras-like small GTP binding proteins regulate a wide variety of intracellular signalling and vesicular trafficking pathways in eukaryotic cells including plant cells. They share a common structure that operates as a molecular switch by cycling between active GTP-bound and inactive GDP-bound conformational states. The active GTP-bound state is regulated by guanine nucleotide exchange factors (GEF), which promote the exchange of GDP for GTP. The inactive GDP-bound state is promoted by GTPase-activating proteins (GAPs) which accelerate GTP hydrolysis by orders of magnitude. Two types of small GTP-binding proteins, ADP-ribosylation factor (Arf) and secretion-associated and Ras-related (Sar), are major regulators of vesicle biogenesis in intracellular traffic and are founding members of a growing family that also includes Arf-related proteins (Arp) and Arf-like (Arl) proteins. The most widely involved small GTPase in vesicular trafficking is probably Arf1, which not only controls assembly of COPI- and AP1, AP3, and AP4/clathrin-coated vesicles but also recruits other proteins to membranes, including some that may be components of further coats. Recent molecular, structural and biochemical studies have provided a wealth of detail of the interactions between Arf and the proteins that regulate its activity as well as providing clues for the types of effector molecules which are controlled by Arf. Sar1 functions as a molecular switch to control the assembly of protein coats (COPII) that direct vesicle budding from ER. The crystallographic analysis of Sar1 reveals a number of structurally unique features that dictate its function in COPII vesicle formation. In this review, I will summarize the current knowledge of Arf and Sar regulation in vesicular trafficking in mammalian and yeast cells and will highlight recent advances in identifying the elements involved in vesicle formation in plant cells. Additionally, I will briefly discuss the similarities and dissimilarities of vesicle traffic in plant, mammalian and yeast cells.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
1664
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15238254-ADP-Ribosylation Factors, pubmed-meshheading:15238254-Arabidopsis, pubmed-meshheading:15238254-Arabidopsis Proteins, pubmed-meshheading:15238254-COP-Coated Vesicles, pubmed-meshheading:15238254-Crystallography, X-Ray, pubmed-meshheading:15238254-Endoplasmic Reticulum, pubmed-meshheading:15238254-Escherichia coli, pubmed-meshheading:15238254-GTP Phosphohydrolases, pubmed-meshheading:15238254-GTP-Binding Proteins, pubmed-meshheading:15238254-GTPase-Activating Proteins, pubmed-meshheading:15238254-Golgi Apparatus, pubmed-meshheading:15238254-Guanine Nucleotide Exchange Factors, pubmed-meshheading:15238254-Guanosine Triphosphate, pubmed-meshheading:15238254-Hydrolysis, pubmed-meshheading:15238254-Membrane Proteins, pubmed-meshheading:15238254-Models, Biological, pubmed-meshheading:15238254-Models, Molecular, pubmed-meshheading:15238254-Molecular Conformation, pubmed-meshheading:15238254-Protein Structure, Secondary, pubmed-meshheading:15238254-R-SNARE Proteins, pubmed-meshheading:15238254-Saccharomyces cerevisiae
pubmed:year
2004
pubmed:articleTitle
The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants.
pubmed:affiliation
TUBITAK, Research Institute for Genetic Engineering and Biotechnology, P.O. Box 21, 41470 Gebze, Kocaeli, Turkey. armemon@rigeb.gov.tr
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't