Linked Life Data

21855798

Source:http://linkedlifedata.com/resource/pubmed/id/21855798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-8-22
pubmed:databankReference
pubmed:abstractText
Liprins are highly conserved scaffold proteins that regulate cell adhesion, cell migration, and synapse development by binding to diverse target proteins. The molecular basis governing liprin/target interactions is poorly understood. The liprin-?2/CASK complex structure solved here reveals that the three SAM domains of liprin-? form an integrated supramodule that binds to the CASK kinase-like domain. As supported by biochemical and cellular studies, the interaction between liprin-? and CASK is unique to vertebrates, implying that the liprin-?/CASK interaction is likely to regulate higher-order brain functions in mammals. Consistently, we demonstrate that three recently identified X-linked mental retardation mutants of CASK are defective in binding to liprin-?. We also solved the liprin-?/liprin-? SAM domain complex structure, which uncovers the mechanism underlying liprin heterodimerizaion. Finally, formation of the CASK/liprin-?/liprin-? ternary complex suggests that liprins can mediate assembly of target proteins into large protein complexes capable of regulating numerous cellular activities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1097-4164
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
586-98
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Liprin-mediated large signaling complex organization revealed by the liprin-?/CASK and liprin-?/liprin-? complex structures.
pubmed:affiliation
Division of Life Science, State Key Laboratory of Molecular Neuroscience, Molecular Neuroscience Center, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't