Document Detail

Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestin-like protein Aly2.
MedLine Citation:
PMID:  20956561     Owner:  NLM     Status:  MEDLINE    
Endocytosis of nutrient transporters is stimulated under various conditions, such as elevated nutrient availability. In Saccharomyces cerevisiae, endocytosis is triggered by ubiquitination of transporters catalyzed by the E3 ubiquitin ligase Rsp5. However, how the ubiquitination is accelerated under certain conditions remains obscure. Here we demonstrate that closely related proteins Aly2/Art3 and Aly1/Art6, which are poorly characterized members of the arrestin-like protein family, mediate endocytosis of the aspartic acid/glutamic acid transporter Dip5. In aly2Δ cells, Dip5 is stabilized at the plasma membrane and is not endocytosed efficiently. Efficient ubiquitination of Dip5 is dependent on Aly2. aly1Δ cells also show deficiency in Dip5 endocytosis, although less remarkably than aly2Δ cells. Aly2 physically interacts in vivo with Rsp5 at its PY motif and also with Dip5, thus serving as an adaptor linking Rsp5 with Dip5 to achieve Dip5 ubiquitination. Importantly, the interaction between Aly2 and Dip5 is accelerated in response to elevated aspartic acid availability. This result indicates that the regulation of Dip5 endocytosis is accomplished by dynamic recruitment of Rsp5 via Aly2.
Riko Hatakeyama; Masao Kamiya; Terunao Takahara; Tatsuya Maeda
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-10-18
Journal Detail:
Title:  Molecular and cellular biology     Volume:  30     ISSN:  1098-5549     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-11-24     Completed Date:  2011-01-13     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5598-607     Citation Subset:  IM    
Institute of Molecular and Cellular Biosciences, University of Tokyo, Tokyo, Japan.
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MeSH Terms
Amino Acid Transport Systems / genetics,  metabolism*
Amino Acid Transport Systems, Basic / genetics,  metabolism
Arrestin / genetics,  metabolism*
Arrestins / genetics,  metabolism*
Aspartic Acid / metabolism
Endocytosis / physiology*
Endosomal Sorting Complexes Required for Transport / genetics,  metabolism*
Recombinant Fusion Proteins / genetics,  metabolism
Saccharomyces cerevisiae / cytology,  metabolism
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Ubiquitin-Protein Ligase Complexes / genetics,  metabolism*
Reg. No./Substance:
0/Aly1 protein, S cerevisiae; 0/Aly2 protein, S cerevisiae; 0/Amino Acid Transport Systems; 0/Amino Acid Transport Systems, Basic; 0/Arrestin; 0/Arrestins; 0/CAN1 protein, S cerevisiae; 0/DIP5 protein, S cerevisiae; 0/Endosomal Sorting Complexes Required for Transport; 0/Recombinant Fusion Proteins; 0/Saccharomyces cerevisiae Proteins; 56-84-8/Aspartic Acid; EC protein, S cerevisiae; EC Ligase Complexes

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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