The unique N‐terminal region of SRMS regulates enzymatic activity and phosphorylation of its novel substrate docking protein 1

• Published in: The FEBS journal Vol. 280; no. 18; pp. 4539 - 4559
• Main Authors: Goel, Raghuveera K., Miah, Sayem, Black, Kristin, Kalra, Natasha, Dai, Chenlu, Lukong, Kiven E.
• Format: Journal Article
• Language: English
• Published: England Blackwell Publishing Ltd 01.09.2013
• Subjects: Bait; breast cancer; Breast Neoplasms - enzymology; Breast Neoplasms - genetics; Breast Neoplasms - pathology; BRK; Carcinoma - enzymology; Carcinoma - genetics; Carcinoma - pathology; Cell Line, Tumor; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Dok1; Female; FRK; Gene Expression Regulation, Neoplastic; Humans; Kinases; Mammary Glands, Human - enzymology; Mammary Glands, Human - pathology; Mutation; Neoplasm Grading; Phosphoproteins - chemistry; Phosphoproteins - genetics; Phosphoproteins - metabolism; Phosphorylation; Protein Binding; Protein Structure, Tertiary; Proteins; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; Signal Transduction; src-Family Kinases - chemistry; src-Family Kinases - genetics; src-Family Kinases - metabolism; SRMS; Transfection; Dok1; breast cancer; BRK; SRMS; FRK

SRMS (Src‐related tyrosine kinase lacking C‐terminal regulatory tyrosine and N‐terminal myristoylation sites) belongs to a family of nonreceptor tyrosine kinases, which also includes breast tumour kinase and Fyn‐related kinase. SRMS, similar to breast tumour kinase and Fyn‐related kinase, harbours a...