DOCK180, a Major CRK-Binding Protein, Alters Cell Morphology upon Translocation to the Cell Membrane

• DOI: 10.1128/mcb.16.4.1770
• Publication Date: 2015-10-09T00:23:17Z
• Authors: Hideki Hasegawa; Etsuko Kiyokawa; Shinya Tanaka; Kazuo Nagashima; Noriko Gotoh; Masabumi Shibuya; Takeshi Kurata; Michiyuki Matsuda
• Keywords: Adapter molecule crk

CRK belongs to a family of adaptor proteins that consist mostly SH2 and SH3 domains. Far Western blotting with has demonstrated it binds 135- 145-, 160-, 180-kDa proteins. The 145-kDa protein is C3G, SH3-binding guanine nucleotide exchange protein. Here, we report on the molecular cloning protein, which designated DOCK180 (180-kDa downstream CRK). isolated cDNA contains 5,598-bp open reading frame encoding an 1,866-amino-acid deduced amino acid sequence did not reveal any significant homology known proteins, except domain was identified at its terminus. To examine function DOCK180, Ki-Ras farnesylation signal fused carboxyl terminus strategy been employed successfully for activation adaptor-binding in vivo. Whereas wild-type accumulated diffusely cytoplasm have effect cell morphology, farnesylated localized cytoplasmic membrane changed spindle 3T3 cells flat, polygonal cells. These results suggest new effector molecule transduces signals from tyrosine kinases through