NCK-interacting protein with SH3 domain is a protein that in humans is encoded by the NCKIPSDgene.[1][2][3]
The protein encoded by this gene is localized exclusively in the cell nucleus. It plays a role in signal transduction, and may function in the maintenance of sarcomeres and in the assembly of myofibrils into sarcomeres. It also plays an important role in stress fiber formation. The gene is involved in therapy-related leukemia by a chromosomal translocation t(3;11)(p21;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified.[3]
↑Sano K, Hayakawa A, Piao JH, Kosaka Y, Nakamura H (Feb 2000). "Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11) (p21;q23)". Blood. 95 (3): 1066–8. PMID10648423.
↑Satoh, S; Tominaga T (Oct 2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". J. Biol. Chem. United States. 276 (42): 39290–4. doi:10.1074/jbc.M107026200. ISSN0021-9258. PMID11509578.
↑Lim, C S; Park E S; Kim D J; Song Y H; Eom S H; Chun J S; Kim J H; Kim J K; Park D; Song W K (Apr 2001). "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation". J. Biol. Chem. United States. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. ISSN0021-9258. PMID11278500.
Hayakawa A, Matsuda Y, Daibata M, et al. (2001). "Genomic organization, tissue expression, and cellular localization of AF3p21, a fusion partner of MLL in therapy-related leukemia". Genes Chromosomes Cancer. 30 (4): 364–74. doi:10.1002/gcc.1102. PMID11241789.
Lim CS, Park ES, Kim DJ, et al. (2001). "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation". J. Biol. Chem. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. PMID11278500.
Satoh S, Tominaga T (2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". J. Biol. Chem. 276 (42): 39290–4. doi:10.1074/jbc.M107026200. PMID11509578.
Lim CS, Kim SH, Jung JG, et al. (2004). "Regulation of SPIN90 phosphorylation and interaction with Nck by ERK and cell adhesion". J. Biol. Chem. 278 (52): 52116–23. doi:10.1074/jbc.M310974200. PMID14559906.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID15324660.
Kim DJ, Kim SH, Lim CS, et al. (2006). "Interaction of SPIN90 with the Arp2/3 complex mediates lamellipodia and actin comet tail formation". J. Biol. Chem. 281 (1): 617–25. doi:10.1074/jbc.M504450200. PMID16253999.
Eisenmann KM, Harris ES, Kitchen SM, et al. (2007). "Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex". Curr. Biol. 17 (7): 579–91. doi:10.1016/j.cub.2007.03.024. PMID17398099.