PRKCI

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PRKCI
Protein PRKCI PDB 1vd2.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRKCI, DXS1179E, PKCI, nPKC-iota, protein kinase C iota
External IDsMGI: 99260 HomoloGene: 37667 GeneCards: PRKCI
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PRKCI
Genomic location for PRKCI
Band3q26.2Start170,222,365 bp[1]
End170,305,981 bp[1]
RNA expression pattern
PBB GE PRKCI 209677 at fs.png

PBB GE PRKCI 213518 at fs.png

PBB GE PRKCI 209678 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002740

NM_008857

RefSeq (protein)

NP_002731

NP_032883

Location (UCSC)Chr 3: 170.22 – 170.31 MbChr 3: 31 – 31.05 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.[5][6][7]

Function[edit]

This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases, the PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent, it is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway, this kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.[7]

Interactions[edit]

PRKCI has been shown to interact with:

[17]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163558 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037643 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Mazzarella R, Ciccodicola A, Esposito T, Arcucci A, Migliaccio C, Jones C, Schlessinger D, D'Urso M, D'Esposito M (Apr 1995). "Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3". Genomics. 26 (3): 629–31. doi:10.1016/0888-7543(95)80190-W. PMID 7607695. 
  6. ^ De Donato M, Gallagher DS, Davis SK, Stelly DM, Taylor JF (April 2002). "The assignment of PRKCI to bovine chromosome 1q34-->q36 by FISH suggests a new assignment to human chromosome 3". Cytogenetics and Cell Genetics. 95 (1–2): 79–81. doi:10.1159/000057021. PMID 11978974. 
  7. ^ a b "Entrez Gene: PRKCI protein kinase C, iota". 
  8. ^ Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A (Aug 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochemical and Biophysical Research Communications. 307 (3): 459–65. doi:10.1016/s0006-291x(03)01187-2. PMID 12893243. 
  9. ^ Lim YP, Low BC, Lim J, Wong ES, Guy GR (Jul 1999). "Association of atypical protein kinase C isotypes with the docker protein FRS2 in fibroblast growth factor signaling". The Journal of Biological Chemistry. 274 (27): 19025–34. doi:10.1074/jbc.274.27.19025. PMID 10383403. 
  10. ^ Tisdale EJ (Feb 2002). "Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway". The Journal of Biological Chemistry. 277 (5): 3334–41. doi:10.1074/jbc.M109744200. PMID 11724794. 
  11. ^ Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Molecular and Cellular Biology. 18 (5): 3069–80. doi:10.1128/mcb.18.5.3069. PMC 110686Freely accessible. PMID 9566925. 
  12. ^ Kohjima M, Noda Y, Takeya R, Saito N, Takeuchi K, Sumimoto H (Dec 2002). "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions". Biochemical and Biophysical Research Communications. 299 (4): 641–6. doi:10.1016/s0006-291x(02)02698-0. PMID 12459187. 
  13. ^ Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (Jul 2000). "A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1". The Journal of Biological Chemistry. 275 (27): 20806–13. doi:10.1074/jbc.M000421200. PMID 10764742. 
  14. ^ Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J (Jan 1996). "Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo". Molecular and Cellular Biology. 16 (1): 105–14. PMC 230983Freely accessible. PMID 8524286. 
  15. ^ Guo W, Wu S, Liu J, Fang B (Sep 2008). "Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota". Cancer Research. 68 (18): 7403–8. doi:10.1158/0008-5472.CAN-08-1449. PMC 2678915Freely accessible. PMID 18794128. 
  16. ^ Ratnayake WS, Apostolatos AH, Ostrov DA, Acevedo-Duncan M (2017). "Two novel atypical PKC inhibitors; ACPD and DNDA effectively mitigate cell proliferation and epithelial to mesenchymal transition of metastatic melanoma while inducing apoptosis". Int. J. Oncol. 51 (5): 1370–1382. doi:10.3892/ijo.2017.4131. PMC 5642393Freely accessible. PMID 29048609. 
  17. ^ Ratnayake WS, Apostolatos CA, Apostolatos AH, Schutte RJ, Huynh MA, Ostrov DA, Acevedo-Duncan M (2018). "Oncogenic PKC-ι activates Vimentin during epithelial-mesenchymal transition in melanoma; a study based on PKC-ι and PKC-ζ specific inhibitors". Cell Adhes. Migr. 0 (0): 1–17. doi:10.1080/19336918.2018.1471323. PMID 29781749. 

Further reading[edit]