Proteolysis-induced N-terminal ectodomain shedding of the integral membrane glycoprotein CUB domain-containing protein 1 (CDCP1) is accompanied by tyrosine phosphorylation of its C-terminal domain and recruitment of Src and PKCδ

Journal of Biological Chemistry

Volumn 285, Issue 34, 2010, Pages 26162-26173

  He, Yaowu ^a   Wortmann, Andreas ^a   Burke, Les J ^a   Reid, Janet C ^a   Adams, Mark N ^a   Abdul Jabbar, Ibtissam ^b   Quigley, James P ^c   Leduc, Richard ^d   Kirchhofer, Daniel ^e   Hooper, John D ^a  

^a QUEENSLAND UNIVERSITY OF TECHNOLOGY   (Australia)

^b UNIVERSITY OF QUEENSLAND   (Australia)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d UNIVERSITÉ DE SHERBROOKE   (Canada)

^e GENENTECH INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL DOMAINS; CELL LINES; CELL SURFACES; CELLULAR PROCESSORS; DOMAIN-CONTAINING PROTEINS; ECTODOMAIN SHEDDING; IMMUNOPURIFICATION; INTEGRAL MEMBRANE; MASS SPECTROSCOPY; N-TERMINAL SEQUENCING; N-TERMINALS; PROTEASE INHIBITOR; PROTEOLYTIC PROCESSING; SERINE PROTEASE; TYROSINE PHOSPHORYLATION; WESTERN BLOTS;

AMINO ACIDS; CELL CULTURE; CELL MEMBRANES; ENZYME ACTIVITY; MASS SPECTROMETRY; PHOSPHATASES; PHOSPHORYLATION;

PROTEINS;

ARGININE; CUB DOMAIN CONTAINING PROTEIN 1; LYSINE; MATRIPTASE; MEMBRANE PROTEIN; PROTEIN KINASE C DELTA; PROTEIN TYROSINE KINASE; PROTEINASE INHIBITOR; SERINE PROTEINASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL SURFACE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MASS SPECTROMETRY; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; REGULATORY MECHANISM; WESTERN BLOTTING;

ANTIGENS, CD; CELL ADHESION MOLECULES; CELL LINE; HUMANS; MEMBRANE GLYCOPROTEINS; NEOPLASM PROTEINS; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN KINASE C-DELTA; PROTEIN TRANSPORT; SERINE PROTEASES; SRC-FAMILY KINASES; TYROSINE;

EID: 77956210264     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.096453     Document Type: Article

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