PRKCI

Last updated
PRKCI
Protein PRKCI PDB 1vd2.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PRKCI , DXS1179E, PKCI, nPKC-iota, protein kinase C iota
External IDs OMIM: 600539 MGI: 99260 HomoloGene: 37667 GeneCards: PRKCI
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 Mb Chr 3: 31.05 – 31.11 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Contents

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. [7]

Interactions

PRKCI has been shown to interact with:

[17]

Related Research Articles

In cell biology, Protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family. PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+). Hence PKC enzymes play important roles in several signal transduction cascades.

<span class="mw-page-title-main">Mitogen-activated protein kinase 9</span> Protein-coding gene in the species Homo sapiens

Mitogen-activated protein kinase 9 is an enzyme that in humans is encoded by the MAPK9 gene.

The PHLPP isoforms are a pair of protein phosphatases, PHLPP1 and PHLPP2, that are important regulators of Akt serine-threonine kinases and conventional/novel protein kinase C (PKC) isoforms. PHLPP may act as a tumor suppressor in several types of cancer due to its ability to block growth factor-induced signaling in cancer cells.

<span class="mw-page-title-main">Protein kinase C zeta type</span>

Protein kinase C, zeta (PKCζ), also known as PRKCZ, is a protein in humans that is encoded by the PRKCZ gene. The PRKCZ gene encodes at least two alternative transcripts, the full-length PKCζ and an N-terminal truncated form PKMζ. PKMζ is thought to be responsible for maintaining long-term memories in the brain. The importance of PKCζ in the creation and maintenance of long-term potentiation was first described by Todd Sacktor and his colleagues at the SUNY Downstate Medical Center in 1993.

<span class="mw-page-title-main">PRKCD</span> Protein-coding gene in the species Homo sapiens

Protein kinase C delta type is an enzyme that in humans is encoded by the PRKCD gene.

<span class="mw-page-title-main">PRKCE</span> Protein-coding gene in the species Homo sapiens

Protein kinase C epsilon type (PKCε) is an enzyme that in humans is encoded by the PRKCE gene. PKCε is an isoform of the large PKC family of protein kinases that play many roles in different tissues. In cardiac muscle cells, PKCε regulates muscle contraction through its actions at sarcomeric proteins, and PKCε modulates cardiac cell metabolism through its actions at mitochondria. PKCε is clinically significant in that it is a central player in cardioprotection against ischemic injury and in the development of cardiac hypertrophy.

<span class="mw-page-title-main">PRKCB1</span> Protein-coding gene in the species Homo sapiens

Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.

<span class="mw-page-title-main">PAWR</span> Protein-coding gene in humans

PRKC apoptosis WT1 regulator protein, or Prostate apoptosis response-4, is a tumor-suppressor protein coded for in the human by the PAWR gene, that induces apoptosis in cancer cells, but not in normal cells.

<span class="mw-page-title-main">Sequestosome 1</span> Protein-coding gene in the species Homo sapiens

Sequestosome-1 is a protein that in humans is encoded by the SQSTM1 gene. Also known as the ubiquitin-binding protein p62, it is an autophagosome cargo protein that targets other proteins that bind to it for selective autophagy. By interacting with GATA4 and targeting it for degradation, it can inhibit GATA-4 associated senescence and senescence-associated secretory phenotype.

<span class="mw-page-title-main">PRKCQ</span> Protein-coding gene in the species Homo sapiens

Protein kinase C theta (PKC-θ) is an enzyme that in humans is encoded by the PRKCQ gene. PKC-θ, a member of serine/threonine kinases, is mainly expressed in hematopoietic cells with high levels in platelets and T lymphocytes, where plays a role in signal transduction. Different subpopulations of T cells vary in their requirements of PKC-θ, therefore PKC-θ is considered as a potential target for inhibitors in the context of immunotherapy.

<span class="mw-page-title-main">Protein kinase D1</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.

<span class="mw-page-title-main">PRKCH</span> Protein-coding gene in the species Homo sapiens

Protein kinase C eta type is an enzyme that in humans is encoded by the PRKCH gene.

<span class="mw-page-title-main">PRKD3</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.

<span class="mw-page-title-main">PRKACB</span> Protein-coding gene in the species Homo sapiens

cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene.

<span class="mw-page-title-main">PARD6A</span> Protein-coding gene in the species Homo sapiens

Partitioning defective 6 homolog alpha is a protein that in humans is encoded by the PARD6A gene.

<span class="mw-page-title-main">MAP2K5</span> Protein-coding gene in the species Homo sapiens

Dual specificity mitogen-activated protein kinase kinase 5 is an enzyme that in humans is encoded by the MAP2K5 gene.

<span class="mw-page-title-main">PRKAG1</span> Protein-coding gene in the species Homo sapiens

5'-AMP-activated protein kinase subunit gamma-1 is an enzyme that in humans is encoded by the PRKAG1 gene.

<span class="mw-page-title-main">SMG1</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase SMG1 is an enzyme that in humans is encoded by the SMG1 gene. SMG1 belongs to the phosphatidylinositol 3-kinase-related kinase protein family.

<span class="mw-page-title-main">PIK3C2G</span> Protein-coding gene in the species Homo sapiens

Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing gamma polypeptide is an enzyme that in humans is encoded by the PIK3C2G gene.

<span class="mw-page-title-main">BIM-1</span> Biological protein kinase C inhibitor

BIM-1 and the related compounds BIM-2, BIM-3, and BIM-8 are bisindolylmaleimide-based protein kinase C (PKC) inhibitors. These inhibitors also inhibit PDK1 explaining the higher inhibitory potential of LY33331 compared to the other BIM compounds a bisindolylmaleimide inhibitor toward PDK1.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000163558 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000037643 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. S2CID   40052490.
  7. 1 2 "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   110686 . 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. doi:10.1128/mcb.16.1.105. PMC   230983 . 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   2678915 . 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   5642393 . 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. 12 (5): 1–17. doi:10.1080/19336918.2018.1471323. PMC   6363030 . PMID   29781749.

Further reading