Protein-tyrosine kinase CAKβ/PYK2 is activated by binding Ca 2+/calmodulin to FERM F2 α2 helix and thus forming its dimer

Biochemical Journal

Volumn 410, Issue 3, 2008, Pages 513-523

  Kohno, Takayuki ^a   Matsuda, Eiko ^a   Sasaki, Hiroko ^a   Sasaki, Terukatsu ^a  

^a SAPPORO MEDICAL UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Calmodulin; Cell adhesion kinase (CAK ); FERM domain; Focal adhesion kinase (FAK); Protein tyrosine kinase; PYK2 (proline rich tyrosine kinase 2); Transphosphorylation

Indexed keywords

BINDING SITES; DIMERS; DNA; ENZYME ACTIVITY; PHOSPHORYLATION;

CALMODULIN; FOCAL ADHESION KINASE (FAK); PROTEIN-TYROSINE KINASE; PYK2 (PROLINE-RICH TYROSINE KINASE 2); TRANSPHOSPHORYLATION;

PROTEINS;

CALCIUM BINDING PROTEIN; CALMODULIN; DIMER; FOCAL ADHESION KINASE 2; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; PROTEIN TYROSINE KINASE;

ARTICLE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; WESTERN BLOTTING;

BASE SEQUENCE; BINDING SITES; BLOTTING, WESTERN; CALCIUM; CALMODULIN; CELL LINE; DIMERIZATION; DNA PRIMERS; DNA, COMPLEMENTARY; ENZYME ACTIVATION; FOCAL ADHESION KINASE 2; HUMANS; PHOSPHORYLATION; TYROSINE; VASOPRESSINS;

EID: 41149130736     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070665     Document Type: Article

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