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词条 PCP4
释义

  1. Function

  2. References

  3. Further reading

{{Infobox_gene}}Purkinje cell protein 4 is a protein that in humans is encoded by the PCP4 gene.[1][2][3] Also known as PEP-19, PCP4 is a 7.6 kDa protein with an IQ-motif that binds to calmodulin (CaM).[4] PCP4 is abundant in Purkinje cells of the cerebellum, and plays an important role in synaptic plasticity.[4][5]

Function

PCP4 knockout mice have been reported to exhibit impaired locomotor learning and markedly altered synaptic plasticity in cerebellar Purkinje neurons.[4] PCP4 accelerates both the association and dissociation of calcium (Ca2+) with calmodulin (CaM), which is postulated to influence the activity of CaM-dependent enzymes, especially CaM kinase II (CaMK-II).[4][6][7]

References

1. ^{{cite journal | vauthors = Chen H, Bouras C, Antonarakis SE | title = Cloning of the cDNA for a human homolog of the rat PEP-19 gene and mapping to chromosome 21q22.2-q22.3 | journal = Hum Genet | volume = 98 | issue = 6 | pages = 672–7 | date = Jan 1997 | pmid = 8931698 | doi = 10.1007/s004390050282 }}
2. ^{{cite journal | vauthors = Cabin DE, Gardiner K, Reeves RH | title = Molecular genetic characterization and comparative mapping of the human PCP4 gene | journal = Somat Cell Mol Genet | volume = 22 | issue = 3 | pages = 167–75 | date = Dec 1996 | pmid = 8914602 | doi = 10.1007/BF02369907 }}
3. ^{{cite web | title = Entrez Gene: PCP4 Purkinje cell protein 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5121| accessdate = }}
4. ^1 2 3 {{cite journal | vauthors = Wei P, Blundon JA, Rong Y, Zakharenko SS, Morgan JI | title = Impaired locomotor learning and altered cerebellar synaptic plasticity in pep-19/PCP4-null mice | journal = Mol. Cell. Biol. | volume = 31 | issue = 14 | pages = 2838–44 | year = 2011 | pmid = 21576365 | pmc = 3133400 | doi = 10.1128/MCB.05208-11 }}
5. ^{{cite journal | vauthors = Sangameswaran L, Hempstead J, Morgan JI | title = Molecular cloning of a neuron-specific transcript and its regulation during normal and aberrant cerebellar development | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 14 | pages = 5651–5 | year = 1989 | pmid = 2748608 | pmc = 297682 | doi = 10.1073/pnas.86.14.5651}}
6. ^{{cite journal | vauthors = Putkey JA, Kleerekoper Q, Gaertner TR, Waxham MN | title = A new role for IQ motif proteins in regulating calmodulin function. | journal = J. Biol. Chem. | volume = 278 | issue = 50 | pages = 49667–70 | year = 2004 | pmid = 14551202 | doi = 10.1074/jbc.C300372200 }}
7. ^{{cite journal | vauthors = Kleerekoper QK, Putkey JA | title = PEP-19, an intrinsically disordered regulator of calmodulin signaling | journal = J. Biol. Chem. | volume = 284 | issue = 12 | pages = 7455–64 | year = 2009 | pmid = 19106096 | pmc = 2658041 | doi = 10.1074/jbc.M808067200 | url = }}

Further reading

{{refbegin|35em}}
  • {{cite journal | vauthors = Hubert RS, Korenberg JR | title = PCP4 maps between D21S345 and P31P10SP6 on chromosome 21q22.2→q22.3. | journal = Cytogenet. Cell Genet. | volume = 78 | issue = 1 | pages = 44–5 | year = 1997 | pmid = 9345904 | doi = 10.1159/000134623 }}
  • {{cite journal | vauthors = Utal AK, Stopka AL, Roy M, Coleman PD | title = PEP-19 immunohistochemistry defines the basal ganglia and associated structures in the adult human brain, and is dramatically reduced in Huntington's disease. | journal = Neuroscience | volume = 86 | issue = 4 | pages = 1055–63 | year = 1998 | pmid = 9697113 | doi = 10.1016/S0306-4522(98)00130-4 }}
  • {{cite journal | vauthors = Hu YH, Warnatz HJ, Vanhecke D, Wagner F, Fiebitz A, Thamm S, Kahlem P, Lehrach H, Yaspo ML, Janitz M | title = Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins. | journal = BMC Genomics | volume = 7 | pages = 155 | year = 2006 | pmid = 16780588 | pmc = 1526728 | doi = 10.1186/1471-2164-7-155 }}
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