Publication Date:
1995-09-29
Description:
Tyrosine-based signals within the cytoplasmic domain of integral membrane proteins mediate clathrin-dependent protein sorting in the endocytic and secretory pathways. A yeast two-hybrid system was used to identify proteins that bind to tyrosine-based signals. The medium chains (mu 1 and mu 2) of two clathrin-associated protein complexes (AP-1 and AP-2, respectively) specifically interacted with tyrosine-based signals of several integral membrane proteins. The interaction was confirmed by in vitro binding assays. Thus, it is likely that the medium chains serve as signal-binding components of the clathrin-dependent sorting machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohno, H -- Stewart, J -- Fournier, M C -- Bosshart, H -- Rhee, I -- Miyatake, S -- Saito, T -- Gallusser, A -- Kirchhausen, T -- Bonifacino, J S -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1872-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569928" target="_blank"〉PubMed〈/a〉
Keywords:
Adaptor Proteins, Vesicular Transport
;
Amino Acid Sequence
;
Cell Membrane/metabolism
;
Clathrin/*metabolism
;
Cloning, Molecular
;
Glutathione Transferase/metabolism
;
Golgi Apparatus/metabolism
;
Lysosomes/metabolism
;
Membrane Proteins/chemistry/*metabolism
;
Molecular Sequence Data
;
Nerve Tissue Proteins/chemistry/*metabolism
;
Phosphoproteins/chemistry/*metabolism
;
Protein Sorting Signals/chemistry/*metabolism
;
Recombinant Fusion Proteins/metabolism
;
Saccharomyces cerevisiae/genetics/metabolism
;
Transformation, Genetic
;
Tyrosine/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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