Identifiers
cyclin-dependent kinase inhibitor 1C (p57, Kip2)
HUGO:CDKN1C, HGNC:1786, ENTREZ:1028, UNIPROT:P49918, GENECARDS:GC11M002904
Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
EMT Senescence / EMT_REGULATORS
EMT Senescence / SENESCENCE
References
PMID:20428755
p57 is a cyclin-dependent kinase (CDK) inhibitor
p57 was initially considered to be a tumor suppressor based on its ability to regulate cell cycle progression
p57 is also involved in the regulation of other cellular processes including transcription, apoptosis, differentiation, development, and migration
The multifunction of p57 participate in many processes in tumorigenesis involving in different mechanisms including regulation of microRNAs
The presence of a nuclear localization signal in p57 is intriguing because it may affect the subcellular localization of p57, which can result in abnormal proliferation and motility of cells, and may be oncogenic under certain circumstances, as observed for p21 and p27
PMID:17464323
Translocation of p57Kip2 to mitochondria occurs within 20 min after staurosporine (apoptotic agent) application.
In fact, p57Kip2 primarily promotes the intrinsic apoptotic pathways, favoring Bax activation and loss of mitochondrial transmembrane potential, consequent release of cytochrome-c into cytosol, caspase-9 and caspase-3 activation.
In accordance, Bcl2 overexpression is able to inhibit p57Kip2 cell death promoting effect.
Thus, in addition to its established function in control of proliferation, these results reveal a mechanism whereby p57Kip2 influences the mitochondrial apoptotic cell death pathway in cancer cells.
References
em_emtc_emtc_re439( EMT Senescence ):
PMID:17464323
Translocation of p57Kip2 to mitochondria occurs within 20 min after staurosporine (apoptotic agent) application.
In fact, p57Kip2 primarily promotes the intrinsic apoptotic pathways, favoring Bax activation and loss of mitochondrial transmembrane potential, consequent release of cytochrome-c into cytosol, caspase-9 and caspase-3 activation.
In accordance, Bcl2 overexpression is able to inhibit p57Kip2 cell death promoting effect.
Thus, in addition to its established function in control of proliferation, these results reveal a mechanism whereby p57Kip2 influences the mitochondrial apoptotic cell death pathway in cancer cells.