Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1997-1-8
pubmed:abstractText
We recently determined that fusion proteins containing tyrosine-based endocytic signals bind to the mu 2 subunit of AP-2, the complex that drives clathrin coat formation and mediates endocytosis from the plasma membrane. Here we analyze the selectivity of peptide recognition by mu 2 and by AP-2 using combinatorial selection methods and surface plasmon resonance. Both mu 2 and AP-2 are shown to interact with various sequences of the form tyrosine-polar-polar-hydrophobic (Yppø) found on receptors that follow the clathrin pathway. The optimal sequence for interaction with mu 2 and with AP-2 has tyrosine as an anchor and prefers arginine at position Y + 2 and leucine at position Y + 3. In contrast, no preferred sequence is detected surrounding the Yppø signal, indicating that recognition of the Yppø endocytic signal does not require a prefolded structure. We conclude that sorting into the endocytic pathway is governed by a surprisingly simple interaction between the mu 2 chain and a tyrosine-containing tetrapeptide sequence.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-1317852, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-1379696, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-1760844, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-1968060, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-2100204, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-2257624, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-2545438, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-2564002, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-2905261, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7511210, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7569928, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7588625, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7671305, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7680435, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7680959, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7706244, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7749194, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7781597, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7814360, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-7822287, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8076832, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8195226, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8280459, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8342026, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8436587, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8491209, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8509395, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8548289, http://linkedlifedata.com/resource/pubmed/commentcorrection/8918456-8647888
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5789-95
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes.
pubmed:affiliation
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't