Biology:PRKCI

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.[1][2][3]

Function

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 phorbol esters 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.[3]

Interactions

PRKCI has been shown to interact with:

[13]


References

  1. "Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3". Genomics 26 (3): 629–31. Apr 1995. doi:10.1016/0888-7543(95)80190-W. PMID 7607695. 
  2. "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. April 2002. doi:10.1159/000057021. PMID 11978974. 
  3. 3.0 3.1 "Entrez Gene: PRKCI protein kinase C, iota". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5584. 
  4. "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochemical and Biophysical Research Communications 307 (3): 459–65. Aug 2003. doi:10.1016/s0006-291x(03)01187-2. PMID 12893243. 
  5. "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. Jul 1999. doi:10.1074/jbc.274.27.19025. PMID 10383403. 
  6. "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. Feb 2002. doi:10.1074/jbc.M109744200. PMID 11724794. 
  7. "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Molecular and Cellular Biology 18 (5): 3069–80. May 1998. doi:10.1128/mcb.18.5.3069. PMID 9566925. 
  8. "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions". Biochemical and Biophysical Research Communications 299 (4): 641–6. Dec 2002. doi:10.1016/s0006-291x(02)02698-0. PMID 12459187. 
  9. "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. Jul 2000. doi:10.1074/jbc.M000421200. PMID 10764742. 
  10. "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. Jan 1996. doi:10.1128/mcb.16.1.105. PMID 8524286. 
  11. "Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota.". Cancer Research 68 (18): 7403–8. Sep 2008. doi:10.1158/0008-5472.CAN-08-1449. PMID 18794128. 
  12. "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. 2017. doi:10.3892/ijo.2017.4131. PMID 29048609. 
  13. "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. 12 (5): 1–17. 2018. doi:10.1080/19336918.2018.1471323. PMID 29781749. 

Further reading