Calsenilin

From Wikipedia, the free encyclopedia

Kv channel interacting protein 3, calsenilin

Identifiers

KCNIP3; CSEN; DREAM; KCHIP3; MGC18289

External IDs

OMIM: 604662 MGI: 1929258 HomoloGene: 8382

Gene ontology
Molecular Function:	• DNA binding • transcription corepressor activity • ion channel activity • voltage-gated ion channel activity • potassium channel activity • calcium ion binding • potassium ion binding
Cellular Component:	• nucleus • membrane
Biological Process:	• transcription • regulation of transcription from RNA polymerase II promoter • ion transport • potassium ion transport • apoptosis • signal transduction

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_001034914 (mRNA)
NP_001030086 (protein)

NM_019789 (mRNA)
NP_062763 (protein)

Location

Chr 2: 95.33 - 95.42 Mb

n/a

Pubmed search

[1]

[2]

Kv channel interacting protein 3, calsenilin, also known as KCNIP3, is a human gene.^[1]

This gene encodes a member of the family of voltage-gated potassium (Kv) channel-interacting proteins, which belong to the recoverin branch of the EF-hand superfamily. 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.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Voltage-gated potassium channel

[edit] References

^ ^a ^b Entrez Gene: KCNIP3 Kv channel interacting protein 3, calsenilin.

[edit] Further reading

Buxbaum JD, Choi EK, Luo Y, et al. (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.
Carrión AM, Mellström B, Naranjo JR (1998). "Protein kinase A-dependent derepression of the human prodynorphin gene via differential binding to an intragenic silencer element.". Mol. Cell. Biol. 18 (12): 6921–9. PMID 9819380.
Carrión AM, Link WA, Ledo F, et al. (1999). "DREAM is a Ca2+-regulated transcriptional repressor.". Nature 398 (6722): 80–4. doi:10.1038/18044. PMID 10078534.
An WF, Bowlby MR, Betty M, et al. (2000). "Modulation of A-type potassium channels by a family of calcium sensors.". Nature 403 (6769): 553–6. doi:10.1038/35000592. PMID 10676964.
Leissring MA, Yamasaki TR, Wasco W, et al. (2000). "Calsenilin reverses presenilin-mediated enhancement of calcium signaling.". Proc. Natl. Acad. Sci. U.S.A. 97 (15): 8590–3. PMID 10900016.
Buxbaum JD, Lilliehook C, Chan JY, et al. (2000). "Genomic structure, expression pattern, and chromosomal localization of the human calsenilin gene: no association between an exonic polymorphism and Alzheimer's disease.". Neurosci. Lett. 294 (3): 135–8. PMID 11072133.
Ledo F, Carrión AM, Link WA, et al. (2001). "DREAM-alphaCREM interaction via leucine-charged domains derepresses downstream regulatory element-dependent transcription.". Mol. Cell. Biol. 20 (24): 9120–6. PMID 11094064.
Jo DG, Kim MJ, Choi YH, et al. (2001). "Pro-apoptotic function of calsenilin/DREAM/KChIP3.". FASEB J. 15 (3): 589–91. doi:10.1096/fj.00-0541fje. PMID 11259376.
Choi EK, Zaidi NF, Miller JS, et al. (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. 276 (22): 19197–204. doi:10.1074/jbc.M008597200. PMID 11278424.
Osawa M, Tong KI, Lilliehook C, et al. (2001). "Calcium-regulated DNA binding and oligomerization of the neuronal calcium-sensing protein, calsenilin/DREAM/KChIP3.". J. Biol. Chem. 276 (44): 41005–13. doi:10.1074/jbc.M105842200. PMID 11535596.
Cheng HY, Pitcher GM, Laviolette SR, et al. (2002). "DREAM is a critical transcriptional repressor for pain modulation.". Cell 108 (1): 31–43. PMID 11792319.
Lilliehook C, Chan S, Choi EK, et al. (2002). "Calsenilin enhances apoptosis by altering endoplasmic reticulum calcium signaling.". Mol. Cell. Neurosci. 19 (4): 552–9. doi:10.1006/mcne.2001.1096. PMID 11988022.
Takimoto K, Yang EK, Conforti L (2002). "Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels.". J. Biol. Chem. 277 (30): 26904–11. doi:10.1074/jbc.M203651200. PMID 12006572.
Ledo F, Kremer L, Mellström B, Naranjo JR (2002). "Ca2+-dependent block of CREB-CBP transcription by repressor DREAM.". EMBO J. 21 (17): 4583–92. PMID 12198160.
Zaidi NF, Berezovska O, Choi EK, et al. (2002). "Biochemical and immunocytochemical characterization of calsenilin in mouse brain.". Neuroscience 114 (1): 247–63. PMID 12207970.
Sanz C, Horita M, Fernandez-Luna JL (2004). "Fas signaling and blockade of Bcr-Abl kinase induce apoptotic Hrk protein via DREAM inhibition in human leukemia cells.". Haematologica 87 (9): 903–7. PMID 12217801.
Schrader LA, Anderson AE, Mayne A, et al. (2002). "PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex.". J. Neurosci. 22 (23): 10123–33. PMID 12451113.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Hong YM, Jo DG, Lee MC, et al. (2003). "Reduced expression of calsenilin/DREAM/KChIP3 in the brains of kainic acid-induced seizure and epilepsy patients.". Neurosci. Lett. 340 (1): 33–6. PMID 12648752.
Shibata R, Misonou H, Campomanes CR, et al. (2003). "A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels.". J. Biol. Chem. 278 (38): 36445–54. doi:10.1074/jbc.M306142200. PMID 12829703.

[edit] External links

MeSH KCNIP3+protein,+human

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v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel