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Gene Review

Snta1  -  syntrophin, acidic 1

Mus musculus

Synonyms: 59 kDa dystrophin-associated protein A1 acidic component 1, AW228934, Alpha-1-syntrophin, Snt1, Syntrophin-1, ...
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Disease relevance of Snta1


High impact information on Snta1


Biological context of Snta1


Anatomical context of Snta1


Associations of Snta1 with chemical compounds


Physical interactions of Snta1

  • Grb2-binding to syntrophin is increased by the addition of either laminin-1 or the isolated laminin alpha1 globular domain modules LG4-5, a protein referred to as E3 [8].
  • Mouse alpha1 syntrophin binds the COOH-terminal domain of dystrophin, and calmodulin inhibits this interaction in a Ca2+-dependent fashion [13].
  • Where calmodulin binds to syntrophin was investigated by constructing fusion proteins containing different regions of syntrophin's sequence [13].
  • In vitro immunoprecipitation and pull-down assays demonstrated that Kir4.1 can bind directly to alpha-syntrophin, requiring the presence of the last three amino acids of the channel (SNV), a consensus PDZ domain-binding motif [16].

Regulatory relationships of Snta1


Other interactions of Snta1


Analytical, diagnostic and therapeutic context of Snta1


  1. Alpha1-syntrophin-deficient skeletal muscle exhibits hypertrophy and aberrant formation of neuromuscular junctions during regeneration. Hosaka, Y., Yokota, T., Miyagoe-Suzuki, Y., Yuasa, K., Imamura, M., Matsuda, R., Ikemoto, T., Kameya, S., Takeda, S. J. Cell Biol. (2002) [Pubmed]
  2. An alpha-syntrophin-dependent pool of AQP4 in astroglial end-feet confers bidirectional water flow between blood and brain. Amiry-Moghaddam, M., Otsuka, T., Hurn, P.D., Traystman, R.J., Haug, F.M., Froehner, S.C., Adams, M.E., Neely, J.D., Agre, P., Ottersen, O.P., Bhardwaj, A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. C-terminal-truncated microdystrophin recruits dystrobrevin and syntrophin to the dystrophin-associated glycoprotein complex and reduces muscular dystrophy in symptomatic utrophin/dystrophin double-knockout mice. Yue, Y., Liu, M., Duan, D. Mol. Ther. (2006) [Pubmed]
  4. Vasomodulation by skeletal muscle-derived nitric oxide requires alpha-syntrophin-mediated sarcolemmal localization of neuronal Nitric oxide synthase. Thomas, G.D., Shaul, P.W., Yuhanna, I.S., Froehner, S.C., Adams, M.E. Circ. Res. (2003) [Pubmed]
  5. Selective loss of sarcolemmal nitric oxide synthase in Becker muscular dystrophy. Chao, D.S., Gorospe, J.R., Brenman, J.E., Rafael, J.A., Peters, M.F., Froehner, S.C., Hoffman, E.P., Chamberlain, J.S., Bredt, D.S. J. Exp. Med. (1996) [Pubmed]
  6. Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution. Adams, M.E., Butler, M.H., Dwyer, T.M., Peters, M.F., Murnane, A.A., Froehner, S.C. Neuron (1993) [Pubmed]
  7. Mouse alpha 1- and beta 2-syntrophin gene structure, chromosome localization, and homology with a discs large domain. Adams, M.E., Dwyer, T.M., Dowler, L.L., White, R.A., Froehner, S.C. J. Biol. Chem. (1995) [Pubmed]
  8. Binding of laminin alpha1-chain LG4-5 domain to alpha-dystroglycan causes tyrosine phosphorylation of syntrophin to initiate Rac1 signaling. Zhou, Y.W., Thomason, D.B., Gullberg, D., Jarrett, H.W. Biochemistry (2006) [Pubmed]
  9. {alpha}-Syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner. Luo, S., Chen, Y., Lai, K.O., Arévalo, J.C., Froehner, S.C., Adams, M.E., Chao, M.V., Ip, N.Y. J. Cell Biol. (2005) [Pubmed]
  10. In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4. Adams, M.E., Mueller, H.A., Froehner, S.C. J. Cell Biol. (2001) [Pubmed]
  11. Differential expression of syntrophins and analysis of alternatively spliced dystrophin transcripts in the mouse brain. Górecki, D.C., Abdulrazzak, H., Lukasiuk, K., Barnard, E.A. Eur. J. Neurosci. (1997) [Pubmed]
  12. Alpha1-syntrophin modulates turnover of ABCA1. Munehira, Y., Ohnishi, T., Kawamoto, S., Furuya, A., Shitara, K., Imamura, M., Yokota, T., Takeda, S., Amachi, T., Matsuo, M., Kioka, N., Ueda, K. J. Biol. Chem. (2004) [Pubmed]
  13. Ca2+-calmodulin binding to mouse alpha1 syntrophin: syntrophin is also a Ca2+-binding protein. Newbell, B.J., Anderson, J.T., Jarrett, H.W. Biochemistry (1997) [Pubmed]
  14. Pleckstrin homology domain 1 of mouse alpha 1-syntrophin binds phosphatidylinositol 4,5-bisphosphate. Chockalingam, P.S., Gee, S.H., Jarrett, H.W. Biochemistry (1999) [Pubmed]
  15. Nitric oxide synthase and cyclic GMP-dependent protein kinase concentrated at the neuromuscular endplate. Chao, D.S., Silvagno, F., Xia, H., Cornwell, T.L., Lincoln, T.M., Bredt, D.S. Neuroscience (1997) [Pubmed]
  16. The potassium channel Kir4.1 associates with the dystrophin-glycoprotein complex via alpha-syntrophin in glia. Connors, N.C., Adams, M.E., Froehner, S.C., Kofuji, P. J. Biol. Chem. (2004) [Pubmed]
  17. Syntrophin is an actin-binding protein the cellular localization of which is regulated through cytoskeletal reorganization in skeletal muscle cells. Iwata, Y., Sampaolesi, M., Shigekawa, M., Wakabayashi, S. Eur. J. Cell Biol. (2004) [Pubmed]
  18. Ultrastructural localization of aquaporin 4 and alpha1-syntrophin in the vascular feet of brain astrocytes. Inoue, M., Wakayama, Y., Liu, J.W., Murahashi, M., Shibuya, S., Oniki, H. Tohoku J. Exp. Med. (2002) [Pubmed]
  19. Interactions between dystrophin glycoprotein complex proteins. Madhavan, R., Jarrett, H.W. Biochemistry (1995) [Pubmed]
  20. Differential effect of alpha-syntrophin knockout on aquaporin-4 and Kir4.1 expression in retinal macroglial cells in mice. Puwarawuttipanit, W., Bragg, A.D., Frydenlund, D.S., Mylonakou, M.N., Nagelhus, E.A., Peters, M.F., Kotchabhakdi, N., Adams, M.E., Froehner, S.C., Haug, F.M., Ottersen, O.P., Amiry-Moghaddam, M. Neuroscience (2006) [Pubmed]
  21. Alpha-syntrophin deletion removes the perivascular but not endothelial pool of aquaporin-4 at the blood-brain barrier and delays the development of brain edema in an experimental model of acute hyponatremia. Amiry-Moghaddam, M., Xue, R., Haug, F.M., Neely, J.D., Bhardwaj, A., Agre, P., Adams, M.E., Froehner, S.C., Mori, S., Ottersen, O.P. FASEB J. (2004) [Pubmed]
  22. The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives. Ahn, A.H., Freener, C.A., Gussoni, E., Yoshida, M., Ozawa, E., Kunkel, L.M. J. Biol. Chem. (1996) [Pubmed]
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