PMC:6085830 / 8766-9927 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/6085830","sourcedb":"PMC","sourceid":"6085830","source_url":"https://www.ncbi.nlm.nih.gov/pmc/6085830","text":"FIGURE 1: The prionlike domain of cellular FUS contains numerous phosphorylation sites. (A) Lysates from multiple human cell lines treated with calicheamicin or calyculin-A showed FUS migrating with a larger apparent molecular weight in Western blot; HEK293T, n = 5; H4, n = 4; U-2 OS, n = 2. (B) Treatment of immunoprecipitated FUS with phosphatase caused FUS to return to its normal apparent size; *Heavy chain of the immunoglobulin G used for immunoprecipitation; n = 2. (C) Substituting glutamate at potential serine or threonine phosphorylation sites caused ectopic FUS in H4 cells to migrate similarly to endogenous FUS from cells treated with calicheamicin or calyculin-A; see Materials and Methods for exact substitution sites; n = 2. (D) Twenty-eight serines and threonines have been identified in this and other studies as putative sites of phosphorylation (bold and underlined; DNA-PK consensus sites are shown in red). Here sites were identified by mass spectrometry following immunoprecipitation of FUS from lysates of human cell lines treated with the DNA-damaging agents calicheamicin or camptothecin, or the phosphatase-inhibitor calyculin-A. ","tracks":[]}