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this study propose that the STRIPAK complex, FAM40A, FAM40B and STRN3, regulates the mode of cancer cell migration by controlling the activity of MST3 and 4, which locally coordinate the phosphorylation of ERM proteins and inhibit the dephosphorylation of MLC leading to increased actin-membrane linkage.
results demonstrate that XBP1 (show XBP1 Proteins) mRNA splicing plays an important role in maintaining the function of bone marrow-derived macrophages and provide new insight into the study and treatment of atherosclerosis
The structure and protein-binding domains of the SG2NA (show STRN Proteins) protein variants have been described.
This result combined with a number of biophysical analyses provide evidence that the coiled coil domain of striatin 3 and the PP2A (show PPP2R4 Proteins) A subunit form a stable core complex with a 2:2 stoichiometry
STRN3 (rs2273171)is associated with single nucleotide polymorphisms in Korean patients, either non-segmental or segmental type.
SG2NA associates with the antioxidant protein (show PRDX3 Proteins) DJ-1 (show PARK7 Proteins) and the survival kinase Akt (show AKT1 Proteins) resulting in resistance to apoptosis induced by oxidative stress.
Results suggest a highly versatile and dynamic mode of regulation of SG2NA with potential implications in tissue development.
Taken together, splicing variation of SG2NA might have some critical roles in differentiation and maturation in metazoan cells.
human homolog is an S, G2 phase nuclear autoantigen detected in a patient with lung and bladder cancer
striatin, calmodulin binding protein 3
, nuclear autoantigen
, cell cycle S/G2 nuclear autoantigen
, cell cycle autoantigen SG2NA
, s/G2 antigen
, SG2NA beta isoform
, striatin-3 35 kDa
, cell-cycle autoantigen SG2NA