Mitogen activated protein kinase phosphatases and cancer
نویسندگان
چکیده
منابع مشابه
Mitogen-Activated Protein Kinases and Mitogen-Activated Protein Kinase Phosphatases in Regenerative Myogenesis and Muscular Dystrophy
متن کامل
Mitogen-activated protein kinase phosphatases inactivate stress-activated protein kinase pathways in vivo.
The c-Jun N-terminal protein kinases (JNKs), also called stress-activated protein kinases, are members of the growing family of serine/threonine kinases in the mitogen-activated protein (MAP) kinase superfamily. Like other MAP kinases, JNKs are activated via phosphorylation on adjacent threonine and tyrosine residues and can be inactivated by a unique family of dual specificity phosphatases, ca...
متن کاملInteraction of Kinase-Interaction-Motif Protein Tyrosine Phosphatases with the Mitogen-Activated Protein Kinase ERK2
The mitogen-activation protein kinase ERK2 is tightly regulated by multiple phosphatases, including those of the kinase interaction motif (KIM) PTP family (STEP, PTPSL and HePTP). Here, we use small angle X-ray scattering (SAXS) and isothermal titration calorimetry (ITC) to show that the ERK2:STEP complex is compact and that residues outside the canonical KIM motif of STEP contribute to ERK2 bi...
متن کاملInactivation of mitogen-activated protein kinase signaling pathway reduces caspase-14 expression in impaired keratinocytes
Objective(s):Several investigations have revealed that caspase-14 is responsible for the epidermal differentiation and cornification, as well as the regulation of moisturizing effect. However, the precise regulation mechanism is still not clear. This study was aimed to investigate the expression of caspase-14 in filaggrin-deficient normal human epidermal keratinocytes (NHEKs) and to explore the...
متن کاملRedox-dependent dimerization of p38α mitogen-activated protein kinase with mitogen-activated protein kinase kinase 3
The kinase p38α MAPK (p38α) plays a pivotal role in many biological processes. p38α is activated by canonical upstream kinases that phosphorylate the activation region. The purpose of our study was to determine whether such activation may depend on redox-sensing cysteines within p38α. p38α was activated and formed a disulfide-bound heterodimer with MAP2K3 (MKK3) in rat cardiomyocytes and isolat...
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ژورنال
عنوان ژورنال: Cancer Biology & Therapy
سال: 2010
ISSN: 1538-4047,1555-8576
DOI: 10.4161/cbt.9.5.11217