rdf:type |
|
lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0033681,
umls-concept:C0033684,
umls-concept:C0086418,
umls-concept:C0332256,
umls-concept:C0439064,
umls-concept:C0439851,
umls-concept:C0851285,
umls-concept:C1150423,
umls-concept:C1552596,
umls-concept:C1947931,
umls-concept:C1956036
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
2000-11-8
|
pubmed:abstractText |
We have identified the multiple PDZ domain containing protein (MUPP-1 or MPDZ) as a novel binding partner of the human c-Kit. c-Kit binds specifically to the 10th PDZ domain of MUPP-1 via its C-terminal sequence. Furthermore, a kinase negative-mutant receptor interacted more strongly with MUPP-1 than the wild-type c-Kit. Strikingly, a constitutively activated c-Kit (D816V-Kit) did not bind to MUPP-1, although this oncogenic form retains the PDZ binding motif 'HDDV' at the C-terminal end. Deletion of V967 of c-Kit abolished binding to MUPP-1 and drastically reduced its tyrosine kinase activity, suggesting that the structure of the C-terminal tail of c-Kit influences its enzymatic activity.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
29
|
pubmed:volume |
482
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
54-8
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
|
pubmed:year |
2000
|
pubmed:articleTitle |
The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity.
|
pubmed:affiliation |
Institut für Biochemie, -OE 4310-, Medizinische Hochschule Hannover, Carl-Neuberg-Str. 1, D-30623 Hannover, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|