SPTBN4 explained
Spectrin, beta, non-erythrocytic 4, also known as SPTBN4, is a protein that in humans is encoded by the SPTBN4 gene.[1] [2]
Spectrin is an actin crosslinking and molecular scaffold protein that links the cell membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. This gene is one member of a family of beta-spectrin genes. The encoded protein localizes to the nuclear matrix, PML nuclear bodies, and cytoplasmic vesicles. A highly similar gene in the mouse is required for localization of specific membrane proteins in polarized regions of neurons. Multiple transcript variants encoding different isoforms have been found for this gene.[1]
Interactions
SPTBN4 has been shown to interact with PTPRN and DISC1.[3]
Further reading
- Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O . Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. . DNA Res. . 7 . 4 . 273–81 . 2001 . 10997877 . 10.1093/dnares/7.4.271 . free .
- Berghs S, Aggujaro D, Dirkx R, Maksimova E, Stabach P, Hermel JM, Zhang JP, Philbrick W, Slepnev V, Ort T, Solimena M . betaIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system. . J. Cell Biol. . 151 . 5 . 985–1002 . 2001 . 11086001 . 2174349 . 10.1083/jcb.151.5.985 .
- Tse WT, Tang J, Jin O, Korsgren C, John KM, Kung AL, Gwynn B, Peters LL, Lux SE . A new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrix. . J. Biol. Chem. . 276 . 26 . 23974–85 . 2001 . 11294830 . 10.1074/jbc.M009307200 . free .
- Komada M, Soriano P . [Beta]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier. . J. Cell Biol. . 156 . 2 . 337–48 . 2002 . 11807096 . 2199236 . 10.1083/jcb.200110003 .
- Shoeman RL, Hartig R, Hauses C, Traub P . Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. . Cell Biol. Int. . 26 . 6 . 529–39 . 2003 . 12119179 . 10.1006/cbir.2002.0895 . 39778155 .
- Nakayama M, Kikuno R, Ohara O . Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs. . Genome Res. . 12 . 11 . 1773–84 . 2003 . 12421765 . 187542 . 10.1101/gr.406902 .
- Ozeki Y, Tomoda T, Kleiderlein J, Kamiya A, Bord L, Fujii K, Okawa M, Yamada N, Hatten ME, Snyder SH, Ross CA, Sawa A . Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth. . Proc. Natl. Acad. Sci. U.S.A. . 100 . 1 . 289–94 . 2003 . 12506198 . 140954 . 10.1073/pnas.0136913100 . 2003PNAS..100..289O . free .
- Morris JA, Kandpal G, Ma L, Austin CP . DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. . Hum. Mol. Genet. . 12 . 13 . 1591–608 . 2004 . 12812986 . 10.1093/hmg/ddg162 . free .
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M . Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. . Cell . 127 . 3 . 635–48 . 2006 . 17081983 . 10.1016/j.cell.2006.09.026 . 7827573 . free .
Notes and References
- Web site: Entrez Gene: SPTBN4 spectrin, beta, non-erythrocytic 4.
- Berghs S, Aggujaro D, Dirkx R, Maksimova E, Stabach P, Hermel JM, Zhang JP, Philbrick W, Slepnev V, Ort T, Solimena M . betaIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system . J. Cell Biol. . 151 . 5 . 985–1002 . November 2000 . 11086001 . 2174349 . 10.1083/jcb.151.5.985 .
- Morris JA, Kandpal G, Ma L, Austin CP . DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation . Hum. Mol. Genet. . 12 . 13 . 1591–608 . Jul 2003 . 12812986 . 10.1093/hmg/ddg162 . free .