Calsenilin

Kv channel interacting protein 3, calsenilin
Identifiers
Symbols KCNIP3; CSEN; DREAM; KCHIP3; MGC18289
External IDs OMIM604662 MGI1929258 HomoloGene8382 GeneCards: KCNIP3 Gene
Orthologs
Species Human Mouse
Entrez 30818 56461
Ensembl ENSG00000115041 ENSMUSG00000079056
UniProt Q9Y2W7 n/a
RefSeq (mRNA) NM_001034914.1 NM_019789
RefSeq (protein) NP_001030086.1 NP_062763
Location (UCSC) Chr 2:
95.96 – 96.05 Mb
Chr 2:
127.28 – 127.35 Mb
PubMed search [1] [2]

Calsenilin is a protein that in humans is encoded by the KCNIP3 gene.[1][2][3]

This gene encodes a member of the family of voltage-gated potassium (Kv) channel-interacting proteins, which belong to the neuronal calcium sensor family of proteins[4][5]. Members of this family are small calcium binding proteins containing EF-hand-like domains. They are integral subunit components of native Kv4 channel complexes that may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium. The encoded protein also functions as a calcium-regulated transcriptional repressor, and interacts with presenilins. Alternatively spliced transcript variants encoding different isoforms have been described.[3]

Contents

Interactions

Calsenilin has been shown to interact with PSEN1[1][6] and PSEN2.[1][7]

See also

References

  1. ^ a b c Buxbaum JD, Choi EK, Luo Y, Lilliehook C, Crowley AC, Merriam DE, Wasco W (Oct 1998). "Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment". Nat Med 4 (10): 1177–81. doi:10.1038/2673. PMID 9771752. 
  2. ^ Carrion AM, Link WA, Ledo F, Mellstrom B, Naranjo JR (Mar 1999). "DREAM is a Ca2+-regulated transcriptional repressor". Nature 398 (6722): 80–4. doi:10.1038/18044. PMID 10078534. 
  3. ^ a b "Entrez Gene: KCNIP3 Kv channel interacting protein 3, calsenilin". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=30818. 
  4. ^ Burgoyne RD (2007). "Neuronal Calcium Sensor Proteins: Generating Diversity in Neuronal Ca2+ Signalling". Nat. Rev. Neurosci. 8 (3): 182–193. doi:10.1038/nrn2093. PMC 1887812. PMID 17311005. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1887812. 
  5. ^ Burgoyne RD, O'Callaghan DW, Hasdemir B, Haynes LP, Tepikin AV (2004). "Neuronal Ca2+-sensor proteins: multitalented regulators of neuronal function". Trends Neurosci. 27 (4): 203–9. doi:10.1016/j.tins.2004.01.010. PMID 15046879. 
  6. ^ Kashiwa, A; Yoshida H, Lee S, Paladino T, Liu Y, Chen Q, Dargusch R, Schubert D, Kimura H (Jul. 2000). "Isolation and characterization of novel presenilin binding protein". J. Neurochem. (UNITED STATES) 75 (1): 109–16. doi:10.1046/j.1471-4159.2000.0750109.x. ISSN 0022-3042. PMID 10854253. 
  7. ^ Choi, E K; Zaidi N F, Miller J S, Crowley A C, Merriam D E, Lilliehook C, Buxbaum J D, Wasco W (Jun. 2001). "Calsenilin is a substrate for caspase-3 that preferentially interacts with the familial Alzheimer's disease-associated C-terminal fragment of presenilin 2". J. Biol. Chem. (United States) 276 (22): 19197–204. doi:10.1074/jbc.M008597200. ISSN 0021-9258. PMID 11278424. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.