Target of rapamycin complex 2 subunit MAPKAP1

Definition:

Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex.

References:

[1]. Jinke Cheng, et al. Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. Mol Cell Biol. 2005 Jul;25(14):5955-64. [Content Brief]

[2]. Wayne A Schroder, et al. Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling. Cell Signal. 2007 Jun;19(6):1279-89. [Content Brief]

[3]. Qian Yang, et al. Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev. 2006 Oct 15;20(20):2820-32. [Content Brief]

[4]. Chieko Makino, et al. Sin1 binds to both ATF-2 and p38 and enhances ATF-2-dependent transcription in an SAPK signaling pathway. Genes Cells. 2006 Nov;11(11):1239-51. [Content Brief]

[5]. Estela Jacinto, et al. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell. 2006 Oct 6;127(1):125-37. [Content Brief]

[6]. Magdalena Cardenas-Rodriguez, et al. The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2 function and interacts with SIN1 to control cilia length independently of the mTOR complex. Hum Mol Genet. 2013 Oct 15;22(20):4031-42. [Content Brief]

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