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Link to original content: http://en.wikipedia.org/wiki/MAPK8IP1
MAPK8IP1 - Wikipedia Jump to content

MAPK8IP1

From Wikipedia, the free encyclopedia

MAPK8IP1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMAPK8IP1, IB1, JIP-1, JIP1, PRKM8IP, mitogen-activated protein kinase 8 interacting protein 1
External IDsOMIM: 604641; MGI: 1309464; HomoloGene: 31314; GeneCards: MAPK8IP1; OMA:MAPK8IP1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005456

NM_001202445
NM_001202446
NM_011162

RefSeq (protein)

NP_005447

NP_001189374
NP_001189375
NP_035292

Location (UCSC)Chr 11: 45.89 – 45.91 MbChr 2: 92.21 – 92.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

C-jun-amino-terminal kinase-interacting protein 1 is an enzyme that in humans is encoded by the MAPK8IP1 gene.[5][6]

The protein encoded by this gene is a regulator of the pancreatic beta-cell function. It is highly similar to JIP-1, a mouse protein known to be a regulator of c-Jun amino-terminal kinase (Mapk8). This protein has been shown to prevent MAPK8 mediated activation of transcription factors, and decrease IL-1 beta and MAP kinase kinase 1 (MEKK1) induced apoptosis in pancreatic beta cells. This protein also functions as a DNA-binding transactivator of the glucose transporter GLUT2. RE1-silencing transcription factor (REST) is reported to repress the expression of this gene in insulin-secreting beta cells. This gene is found to be mutated in a type 2 diabetes family, and thus is thought to be a susceptibility gene for type 2 diabetes.[7]

Interactions

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MAPK8IP1 has been shown to interact with MAP3K10,[8] DUSP16,[9] Mitogen-activated protein kinase 9,[8][10] MAPK8,[10][11] LRP2,[12][13] LRP1,[12] MAP3K12,[8] MAP2K7,[8] MAPK8IP2[8] and MAP3K11.[8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000121653Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027223Ensembl, 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. ^ Dickens M, Rogers JS, Cavanagh J, Raitano A, Xia Z, Halpern JR, Greenberg ME, Sawyers CL, Davis RJ (August 1997). "A cytoplasmic inhibitor of the JNK signal transduction pathway". Science. 277 (5326): 693–6. doi:10.1126/science.277.5326.693. PMID 9235893.
  6. ^ Bonny C, Nicod P, Waeber G (March 1998). "IB1, a JIP-1-related nuclear protein present in insulin-secreting cells". J Biol Chem. 273 (4): 1843–6. doi:10.1074/jbc.273.4.1843. PMID 9442013.
  7. ^ "Entrez Gene: MAPK8IP1 mitogen-activated protein kinase 8 interacting protein 1".
  8. ^ a b c d e f Yasuda J, Whitmarsh A J, Cavanagh J, Sharma M, Davis R J (October 1999). "The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins". Mol. Cell. Biol. 19 (10): 7245–54. doi:10.1128/mcb.19.10.7245. ISSN 0270-7306. PMC 84717. PMID 10490659.
  9. ^ Willoughby EA, Perkins Gordon R, Collins Mary K, Whitmarsh Alan J (March 2003). "The JNK-interacting protein-1 scaffold protein targets MAPK phosphatase-7 to dephosphorylate JNK". J. Biol. Chem. 278 (12): 10731–6. doi:10.1074/jbc.M207324200. ISSN 0021-9258. PMID 12524447.
  10. ^ a b Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis R J (September 1998). "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science. 281 (5383): 1671–4. Bibcode:1998Sci...281.1671W. doi:10.1126/science.281.5383.1671. ISSN 0036-8075. PMID 9733513.
  11. ^ Cai Y, Lechner Mark S, Nihalani Deepak, Prindle Marc J, Holzman Lawrence B, Dressler Gregory R (January 2002). "Phosphorylation of Pax2 by the c-Jun N-terminal kinase and enhanced Pax2-dependent transcription activation". J. Biol. Chem. 277 (2): 1217–22. doi:10.1074/jbc.M109663200. ISSN 0021-9258. PMID 11700324.
  12. ^ a b Gotthardt M, Trommsdorff M, Nevitt M F, Shelton J, Richardson J A, Stockinger W, Nimpf J, Herz J (August 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. ISSN 0021-9258. PMID 10827173.
  13. ^ Petersen HH, Hilpert Jan, Militz Daniel, Zandler Valerie, Jacobsen Christian, Roebroek Anton J M, Willnow Thomas E (February 2003). "Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule". J. Cell Sci. 116 (Pt 3): 453–61. doi:10.1242/jcs.00243. ISSN 0021-9533. PMID 12508107.

Further reading

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