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10.1074/jbc.RA120.014464 http://scihub22266oqcxt.onion/10.1074/jbc.RA120.014464 32571875!7450121!32571875     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2020 ; 295 (33): 11682-11692 Nephropedia Template TP {{tp|p=32571875|t=2020. PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth |pdf=|usr=}}{{32571875}} gab.com Text PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=32571875 #FOAvip Phosphatases of regenerating liver (PRLs) are markers of cancer and promote tumor growth. They have been implicated in a variety of biochemical pathways but the physiologically relevant target of phosphatase activity has eluded 20 years of investigation. Here, we show that PRL3 catalytic activity is not required in a mouse model of metastasis. PRL3 binds and inhibits CNNM4, a membrane protein associated with magnesium transport. Analysis of PRL3 mutants specifically defective in either CNNM-binding or phosphatase activity demonstrate that CNNM binding is necessary and sufficient to promote tumor metastasis. As PRLs do have phosphatase activity, they are in fact pseudo-pseudophosphatases. Phosphatase activity leads to formation of phosphocysteine, which blocks CNNM binding and may play a regulatory role. We show levels of PRL cysteine phosphorylation vary in response to culture conditions and in different tissues. Examination of related protein phosphatases shows the stability of phosphocysteine is a unique and evolutionarily conserved property of PRLs. The demonstration that PRL3 functions as a pseudophosphatase has important ramifications for the design of PRL inhibitors for cancer. Twit Text FOAVip PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=32571875 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32571875 #FOAvip English Wikipedia <ref>{{Cite pmid|32571875}}</ref> PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth #MMPMID32571875 Kozlov G; Funato Y; Chen YS; Zhang Z; Illes K; Miki H; Gehring K J Biol Chem 2020[Aug]; 295 (33): 11682-11692 PMID32571875show ga Phosphatases of regenerating liver (PRLs) are markers of cancer and promote tumor growth. They have been implicated in a variety of biochemical pathways but the physiologically relevant target of phosphatase activity has eluded 20 years of investigation. Here, we show that PRL3 catalytic activity is not required in a mouse model of metastasis. PRL3 binds and inhibits CNNM4, a membrane protein associated with magnesium transport. Analysis of PRL3 mutants specifically defective in either CNNM-binding or phosphatase activity demonstrate that CNNM binding is necessary and sufficient to promote tumor metastasis. As PRLs do have phosphatase activity, they are in fact pseudo-pseudophosphatases. Phosphatase activity leads to formation of phosphocysteine, which blocks CNNM binding and may play a regulatory role. We show levels of PRL cysteine phosphorylation vary in response to culture conditions and in different tissues. Examination of related protein phosphatases shows the stability of phosphocysteine is a unique and evolutionarily conserved property of PRLs. The demonstration that PRL3 functions as a pseudophosphatase has important ramifications for the design of PRL inhibitors for cancer. |Animals[MESH] |COS Cells[MESH] |Carcinogenesis/genetics/*metabolism/pathology[MESH] |Chlorocebus aethiops[MESH] |Female[MESH] |HEK293 Cells[MESH] |HeLa Cells[MESH] |Humans[MESH] |Immediate-Early Proteins/chemistry/genetics/*metabolism[MESH] |Magnesium/metabolism[MESH] |Melanoma, Experimental/genetics/metabolism/pathology[MESH] |Mice, Inbred C57BL[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Neoplasm Metastasis/genetics/pathology[MESH] |Neoplasm Proteins/chemistry/genetics/*metabolism[MESH]PRL3 pseudophosphatase activity is necessary and sufficient to promote(epmc).pdf DeepDyve Pubget Overpricing