Mass spectrometry identification and systems analysis of cytosolic protein N- lysine methylation in anucleate blood platelets

ABSTRACT: Here, we characterize the methyl-lysine (meK) proteome of anucleate blood platelets. With high-resolution, multiplex mass spectrometry methods, we identify 190 mono-, di- and tri-meK modifications on 150 different platelet proteins, including 28 quantifiable meK modifications consistently present in platelets from multiple individuals. In addition to identifying meK modifications on calmodulin (CaM), GRP78 and EF1A1 that have been previously characterized in other cell types, we also uncover more novel modifications on numerous other cytosolic proteins. Together, our results and analyses support roles for lysine methylation in mediating cytoskeletal, translational, secretory and other cytosolic cellular processes.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Platelet, Platelet

DISEASE(S): Disease Free

SUBMITTER: Phillip Wilmarth  

LAB HEAD: Dr. Joseph E. Aslan

PROVIDER: PXD012217 | Pride | 2019-04-18

REPOSITORIES: Pride