BACKGROUND: In the mouse submembranous protein tyrosine phosphatase PTP-BL five PDZ domains are present in between the N-terminal FERM domain, which directs the protein to the cell cortex, and the C-terminal catalytic phosphatase domain. To understand more on the physical role of PTP-BL in this microenvironment, we started to search for PTP-BL PDZ domain-interacting proteins. RESULTS: Yeast two-hybrid screening for PTP-BL targets resulted in the identification of a novel mouse LIM-only protein termed CRIP2 that is highly homologous to rat ESP1 and human CRP2 sequences. Mouse CRIP2 has a predicted molecular weight of 23 kD and consists of two LIM domains spaced by 68 amino acids. The fourth PDZ domain of PTP-BL is responsible for the binding of CRIP2 protein. Both PTP-BL and CRIP2 mRNAs display a wide, overlapping tissue distribution. Western blot analysis revealed a more restricted expression pattern for CRIP2 with high expression in lung, heart and brain. CRIP2 protein is localized at cell cortical, actin-rich structures, which is concurrent with the subcellular localization of PTP-BL. CONCLUSIONS: The observed characteristics of the LIM domain-containing adaptor protein CRIP2 are consistent with a potential role of PTP-BL in the dynamics of the cortical actin cytoskeleton.
BACKGROUND: In the mouse submembranous protein tyrosine phosphatase PTP-BL five PDZ domains are present in between the N-terminal FERM domain, which directs the protein to the cell cortex, and the C-terminal catalytic phosphatase domain. To understand more on the physical role of PTP-BL in this microenvironment, we started to search for PTP-BL PDZ domain-interacting proteins. RESULTS: Yeast two-hybrid screening for PTP-BL targets resulted in the identification of a novel mouse LIM-only protein termed CRIP2 that is highly homologous to ratESP1 and humanCRP2 sequences. MouseCRIP2 has a predicted molecular weight of 23 kD and consists of two LIM domains spaced by 68 amino acids. The fourth PDZ domain of PTP-BL is responsible for the binding of CRIP2 protein. Both PTP-BL and CRIP2 mRNAs display a wide, overlapping tissue distribution. Western blot analysis revealed a more restricted expression pattern for CRIP2 with high expression in lung, heart and brain. CRIP2 protein is localized at cell cortical, actin-rich structures, which is concurrent with the subcellular localization of PTP-BL. CONCLUSIONS: The observed characteristics of the LIM domain-containing adaptor protein CRIP2 are consistent with a potential role of PTP-BL in the dynamics of the cortical actin cytoskeleton.
Authors: Lieke C J van den Berk; Marco A van Ham; Mariska M te Lindert; Tine Walma; Jan Aelen; Geerten W Vuister; Wiljan J A J Hendriks Journal: Mol Biol Rep Date: 2004-12 Impact factor: 2.316
Authors: Colleen A Brady; Dadi Jiang; Stephano S Mello; Thomas M Johnson; Lesley A Jarvis; Margaret M Kozak; Daniela Kenzelmann Broz; Shashwati Basak; Eunice J Park; Margaret E McLaughlin; Anthony N Karnezis; Laura D Attardi Journal: Cell Date: 2011-05-13 Impact factor: 41.582
Authors: Jessica C Amlin-Van Schaick; Sungjin Kim; Christina DiFabio; Min-Hyung Lee; Karl W Broman; Karlyne M Reilly Journal: Neuro Oncol Date: 2012-01-10 Impact factor: 12.300
Authors: Arthur Kwok Leung Cheung; Josephine M Y Ko; Hong Lok Lung; Kwok Wah Chan; Eric J Stanbridge; Eugene Zabarovsky; Takashi Tokino; Lisa Kashima; Toshiharu Suzuki; Dora Lai-Wan Kwong; Daniel Chua; Sai Wah Tsao; Maria Li Lung Journal: Proc Natl Acad Sci U S A Date: 2011-05-03 Impact factor: 11.205
Authors: Guillermo U Ruiz-Esparza; Jose H Flores-Arredondo; Victor Segura-Ibarra; Guillermo Torre-Amione; Mauro Ferrari; Elvin Blanco; Rita E Serda Journal: Int J Nanomedicine Date: 2013-02-09