MAP3K10

From Wikipedia, the free encyclopedia

Mitogen-activated protein kinase kinase kinase 10

Identifiers

MAP3K10; MLK2; MST

External IDs

OMIM: 600137 MGI: 1346879 HomoloGene: 1834

Gene ontology
Molecular Function:	• nucleotide binding • transcription corepressor activity • protein serine/threonine kinase activity • JUN kinase kinase kinase activity • protein-tyrosine kinase activity • protein binding • ATP binding • transferase activity • protein homodimerization activity
Biological Process:	• induction of apoptosis • signal transduction • activation of JNK activity • negative regulation of transcription • protein amino acid autophosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_002446 (mRNA)
NP_002437 (protein)

XM_001000402 (mRNA)
XP_001000402 (protein)

Location

Chr 19: 45.39 - 45.41 Mb

Chr 7: 27.37 - 27.38 Mb

Pubmed search

[1]

[2]

Mitogen-activated protein kinase kinase kinase 10, also known as MAP3K10, is a human gene.^[1]

The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase has been shown to activate MAPK8/JNK and MKK4/SEK1, and this kinase itself can be phoshorylated, and thus activated by JNK kinases. This kinase functions preferentially on the JNK signaling pathway, and is reported to be involved in nerve growth factor (NGF) induced neuronal apoptosis.^[1]

[edit] References

^ ^a ^b Entrez Gene: MAP3K10 mitogen-activated protein kinase kinase kinase 10.

[edit] Further reading

Katoh M, Hirai M, Sugimura T, Terada M (1995). "Cloning and characterization of MST, a novel (putative) serine/threonine kinase with SH3 domain.". Oncogene 10 (7): 1447-51. PMID 7731697.
Gallo KA, Mark MR, Scadden DT, et al. (1994). "Identification and characterization of SPRK, a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity.". J. Biol. Chem. 269 (21): 15092-100. PMID 8195146.
Dorow DS, Devereux L, Dietzsch E, De Kretser T (1993). "Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains.". Eur. J. Biochem. 213 (2): 701-10. PMID 8477742.
Dorow DS, Devereux L, Tu GF, et al. (1996). "Complete nucleotide sequence, expression, and chromosomal localisation of human mixed-lineage kinase 2.". Eur. J. Biochem. 234 (2): 492-500. PMID 8536694.
Hirai S, Katoh M, Terada M, et al. (1997). "MST/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase/stress-activated protein kinase.". J. Biol. Chem. 272 (24): 15167-73. PMID 9182538.
Nagata K, Puls A, Futter C, et al. (1998). "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3.". EMBO J. 17 (1): 149-58. doi:10.1093/emboj/17.1.149. PMID 9427749.
Hirai S, Noda K, Moriguchi T, et al. (1998). "Differential activation of two JNK activators, MKK7 and SEK1, by MKN28-derived nonreceptor serine/threonine kinase/mixed lineage kinase 2.". J. Biol. Chem. 273 (13): 7406-12. PMID 9516438.
Rasmussen RK, Ji H, Eddes JS, et al. (1998). "Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins.". Electrophoresis 19 (5): 809-17. doi:10.1002/elps.1150190535. PMID 9629920.
Rasmussen RK, Rusak J, Price G, et al. (1998). "Mixed-lineage kinase 2-SH3 domain binds dynamin and greatly enhances activation of GTPase by phospholipid.". Biochem. J. 335 ( Pt 1): 119-24. PMID 9742220.
Liu YF, Dorow D, Marshall J (2000). "Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin.". J. Biol. Chem. 275 (25): 19035-40. doi:10.1074/jbc.C000180200. PMID 10801775.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788-95. PMID 11076863.
Savinainen A, Garcia EP, Dorow D, et al. (2001). "Kainate receptor activation induces mixed lineage kinase-mediated cellular signaling cascades via post-synaptic density protein 95.". J. Biol. Chem. 276 (14): 11382-6. doi:10.1074/jbc.M100190200. PMID 11152698.
Xu Z, Maroney AC, Dobrzanski P, et al. (2001). "The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis.". Mol. Cell. Biol. 21 (14): 4713-24. doi:10.1128/MCB.21.14.4713-4724.2001. PMID 11416147.
Poy MN, Yang Y, Rezaei K, et al. (2002). "CEACAM1 regulates insulin clearance in liver.". Nat. Genet. 30 (3): 270-6. doi:10.1038/ng840. PMID 11850617.
Akbarzadeh S, Ji H, Frecklington D, et al. (2002). "Mixed lineage kinase 2 interacts with clathrin and influences clathrin-coated vesicle trafficking.". J. Biol. Chem. 277 (39): 36280-7. doi:10.1074/jbc.M204626200. PMID 12105200.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Figueroa C, Tarras S, Taylor J, Vojtek AB (2004). "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex.". J. Biol. Chem. 278 (48): 47922-7. doi:10.1074/jbc.M307357200. PMID 14504284.
Eckey M, Tenbaum SP, Muñoz A, Baniahmad A (2004). "Mixed lineage kinase 2 enhances trans-repression of Alien and nuclear receptors.". Mol. Cell. Endocrinol. 213 (1): 71-8. doi:10.1016/j.mce.2003.10.035. PMID 15062575.
Jaffe AB, Hall A, Schmidt A (2005). "Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho.". Curr. Biol. 15 (5): 405-12. doi:10.1016/j.cub.2004.12.082. PMID 15753034.
Kollers S, Musilova P, Rubes J, Rocha D (2007). "Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13.". Anim. Genet. 37 (6): 595-6. doi:10.1111/j.1365-2052.2006.01516.x. PMID 17121608.