SNTA1

From Wikipedia, the free encyclopedia

Syntrophin, alpha 1 (dystrophin-associated protein A1, 59kDa, acidic component)

PDB rendering based on 1qav.

Available structures: 1qav, 1z86, 1z87, 2pdz

Identifiers

Symbol(s)

SNTA1; SNT1; TACIP1; dJ1187J4.5

External IDs

OMIM: 601017 MGI: 101772 HomoloGene: 2331

Gene ontology
Molecular Function:	• actin binding • calcium ion binding • calmodulin binding
Cellular Component:	• cytoskeleton • postsynaptic membrane
Biological Process:	• muscle contraction • neuromuscular junction development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003098 (mRNA)
NP_003089 (protein)

NM_009228 (mRNA)
NP_033254 (protein)

Location

Chr 20: 31.46 - 31.5 Mb

Chr 2: 154.07 - 154.1 Mb

Pubmed search

[1]

[2]

Syntrophin, alpha 1 (dystrophin-associated protein A1, 59kDa, acidic component), also known as SNTA1, is a human gene.^[1]

Dystrophin is a large, rod-like cytoskeletal protein found at the inner surface of muscle fibers. Dystrophin is missing in Duchenne Muscular Dystrophy patients and is present in reduced amounts in Becker Muscular Dystrophy patients. The protein encoded by this gene is a peripheral membrane protein found associated with dystrophin and dystrophin-related proteins. This gene is a member of the syntrophin gene family, which contains at least two other structurally-related genes.^[1]

[edit] References

^ ^a ^b Entrez Gene: SNTA1 syntrophin, alpha 1 (dystrophin-associated protein A1, 59kDa, acidic component).

[edit] Further reading

Miyagoe-Suzuki Y, Takeda SI (2002). "Association of neuronal nitric oxide synthase (nNOS) with alpha1-syntrophin at the sarcolemma.". Microsc. Res. Tech. 55 (3): 164–70. doi:10.1002/jemt.1167. PMID 11747091.
Blake DJ (2002). "Dystrobrevin dynamics in muscle-cell signalling: a possible target for therapeutic intervention in Duchenne muscular dystrophy?". Neuromuscul. Disord. 12 Suppl 1: S110–7. PMID 12206805.
Yang B, Jung D, Rafael JA, et al. (1995). "Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin.". J. Biol. Chem. 270 (10): 4975–8. PMID 7890602.
Ahn AH, Freener CA, Gussoni E, et al. (1996). "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives.". J. Biol. Chem. 271 (5): 2724–30. PMID 8576247.
Castelló A, Brochériou V, Chafey P, et al. (1996). "Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast.". FEBS Lett. 383 (1-2): 124–8. PMID 8612778.
Gee SH, Madhavan R, Levinson SR, et al. (1998). "Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins.". J. Neurosci. 18 (1): 128–37. PMID 9412493.
Iwata Y, Pan Y, Yoshida T, et al. (1998). "Alpha1-syntrophin has distinct binding sites for actin and calmodulin.". FEBS Lett. 423 (2): 173–7. PMID 9512352.
Hasegawa M, Cuenda A, Spillantini MG, et al. (1999). "Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition.". J. Biol. Chem. 274 (18): 12626–31. PMID 10212242.
Hillier BJ, Christopherson KS, Prehoda KE, et al. (1999). "Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex.". Science 284 (5415): 812–5. PMID 10221915.
Fernández-Larrea J, Merlos-Suárez A, Ureña JM, et al. (1999). "A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface.". Mol. Cell 3 (4): 423–33. PMID 10230395.
Lumeng C, Phelps S, Crawford GE, et al. (1999). "Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases.". Nat. Neurosci. 2 (7): 611–7. doi:10.1038/10165. PMID 10404183.
Adams ME, Kramarcy N, Krall SP, et al. (2000). "Absence of alpha-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin.". J. Cell Biol. 150 (6): 1385–98. PMID 10995443.
Newey SE, Benson MA, Ponting CP, et al. (2001). "Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex.". Curr. Biol. 10 (20): 1295–8. PMID 11069112.
Olalla L, Aledo JC, Bannenberg G, Márquez J (2001). "The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins.". FEBS Lett. 488 (3): 116–22. PMID 11163757.
Marchand S, Stetzkowski-Marden F, Cartaud J (2001). "Differential targeting of components of the dystrophin complex to the postsynaptic membrane.". Eur. J. Neurosci. 13 (2): 221–9. PMID 11168526.
Xu H, Goldfarb M (2001). "Multiple effector domains within SNT1 coordinate ERK activation and neuronal differentiation of PC12 cells.". J. Biol. Chem. 276 (16): 13049–56. doi:10.1074/jbc.M009925200. PMID 11278583.
Hogan A, Shepherd L, Chabot J, et al. (2001). "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions.". J. Biol. Chem. 276 (28): 26526–33. doi:10.1074/jbc.M104156200. PMID 11352924.
Oak SA, Russo K, Petrucci TC, Jarrett HW (2001). "Mouse alpha1-syntrophin binding to Grb2: further evidence of a role for syntrophin in cell signaling.". Biochemistry 40 (37): 11270–8. PMID 11551227.
Adams ME, Mueller HA, Froehner SC (2001). "In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4.". J. Cell Biol. 155 (1): 113–22. doi:10.1083/jcb.200106158. PMID 11571312.
Neely JD, Amiry-Moghaddam M, Ottersen OP, et al. (2002). "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein.". Proc. Natl. Acad. Sci. U.S.A. 98 (24): 14108–13. doi:10.1073/pnas.241508198. PMID 11717465.