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rdf:type |
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lifeskim:mentions |
umls-concept:C0055857,
umls-concept:C0085828,
umls-concept:C0205145,
umls-concept:C0475311,
umls-concept:C0524637,
umls-concept:C0919496,
umls-concept:C0968902,
umls-concept:C1552644,
umls-concept:C1705552,
umls-concept:C1823153,
umls-concept:C2003941,
umls-concept:C2349976
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pubmed:issue |
5
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pubmed:dateCreated |
2007-4-23
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pubmed:abstractText |
The clathrin adaptors AP-1 and AP-2 bind cargo proteins via two types of motifs: tyrosine-based Yxx phi and dileucine-based [DE]XXXL[LI]. Although it is well established that Yxx phi motifs bind to the mu subunits of AP-1 or AP-2, dileucine motifs have been reported to bind to either the mu or beta subunits of these adaptors as well as the gamma/sigma1 hemicomplex of AP-1. To clarify this controversy, the various subunits of AP-1 and AP-2 were expressed individually and in hemicomplex form in insect cells, and they were used in glutathione S-transferase pull-down assays to determine their binding properties. We report that the gamma/sigma1 or alpha/sigma2 hemicomplexes bound the dileucine-based motifs of several proteins quite strongly, whereas binding by the beta1/mu1 and beta2/mu2 hemicomplexes, and the individual beta or mu subunits, was extremely weak or undetectable. The gamma/sigma1 and alpha/sigma2 hemicomplexes displayed substantial differences in their preference for particular dileucine-based motifs. Most strikingly, an aspartate at position -4 compromised binding to the gamma/sigma1 hemicomplex, whereas minimally affecting binding to alpha/sigma2. There was an excellent correlation between binding to the alpha/sigma2 hemicomplex and in vivo internalization mediated by the dileucine-based sorting signals. These findings provide new insights into the trafficking mechanisms of D/EXXXL[LI]-mediated sorting signals.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-10593899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-10747918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-10814565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-10973972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-11123907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-11382783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-11387476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-11451993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-12058068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-12370188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-12651740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-1317852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-14555962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-14608369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-14691137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-14973137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-15158672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-15377783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-15681409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-16162817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-16439540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-16723738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-17267500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-7569928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-7593184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-7790352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-8537368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-9497313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-9545228,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-9811611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17360967-9812899
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1887-96
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17360967-Adaptor Protein Complex 1,
pubmed-meshheading:17360967-Adaptor Protein Complex 2,
pubmed-meshheading:17360967-Amino Acid Motifs,
pubmed-meshheading:17360967-Amino Acid Sequence,
pubmed-meshheading:17360967-Animals,
pubmed-meshheading:17360967-Binding Sites,
pubmed-meshheading:17360967-CHO Cells,
pubmed-meshheading:17360967-Cricetinae,
pubmed-meshheading:17360967-Cricetulus,
pubmed-meshheading:17360967-Dipeptides,
pubmed-meshheading:17360967-Green Fluorescent Proteins,
pubmed-meshheading:17360967-Humans,
pubmed-meshheading:17360967-Mice,
pubmed-meshheading:17360967-Multiprotein Complexes,
pubmed-meshheading:17360967-Protein Sorting Signals,
pubmed-meshheading:17360967-Recombinant Fusion Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site.
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pubmed:affiliation |
Department of Internal Medicine and Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, N.I.H., Extramural
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