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PMID: 9820800 Published · ppublish English Journal Article Review

Molecular aspects of the endocytic pathway.

The Biochemical journal ·Vol. 336 ( Pt 2) ·1998-12-01 ·Pages 271-82

Clague MJ

Abstract

Observation of the flow of material along the endocytic pathway has lead to the description of the basic architecture of the pathway and provided insight into the relationship between compartments. Significant advances have been made in the study of endocytic transport steps at the molecular level, of which studies of cargo selection, vesicle budding and membrane fusion events comprise the major part. Progress in this area has been driven by two approaches, yeast genetics and in vitro or cell-free assays, which reconstitute particular transport steps and allow biochemical manipulation. The complex protein machineries that control vesicle budding and fusion are significantly conserved between the secretory and endocytic pathways such that proteins that regulate particular steps are often part of a larger family of proteins which exercise a conserved function at other locations within the cell. Well characterized examples include vesicle coat proteins, rabs (small GTPases) and soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (SNAP) receptors (SNAREs). Intracompartmental pH, lipid composition and cytoskeletal organization have also been identified as important determinants of the orderly flow of material within the endocytic pathway.

MeSH Terms
Adenosine Triphosphatases/metabolism Animals Biological Transport Cell Fusion Cytoskeleton Endocytosis/physiology Endosomes/metabolism GTP Phosphohydrolases/metabolism GTP-Binding Proteins/metabolism Humans Lipid Metabolism Phosphatidylinositol 3-Kinases/metabolism Proteins/metabolism Saccharomyces cerevisiae Proteins Vacuoles/metabolism rab GTP-Binding Proteins
Chemicals
Proteins Saccharomyces cerevisiae Proteins Phosphatidylinositol 3-Kinases Adenosine Triphosphatases GTP Phosphohydrolases GTP-Binding Proteins YPT1 protein, S cerevisiae rab GTP-Binding Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Clague M J
Physiological Laboratory, University of Liverpool, Crown Street, Liverpool L69 3BX, U.K. clague@liv.ac.uk
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj3360271
Email
clague@liv.ac.uk
Published
1998-12-01
Pages
271-82
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1219867
Subset
IM
External Links
PubMed source DOI: 10.1042/bj3360271 PMC Full Text View journal details
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