Proteomics

Dataset Information

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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): Orbitrap Fusion ETD

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

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Publications

Identification, Quantification, and System Analysis of Protein N-ε Lysine Methylation in Anucleate Blood Platelets.

Rocheleau Anne D AD   Melrose Alexander R AR   Cunliffe Jennifer M JM   Klimek John J   Babur Özgün Ö   Tassi Yunga Samuel S   Ngo Anh T P ATP   Pang Jiaqing J   David Larry L LL   McCarty Owen J T OJT   Aslan Joseph E JE  

Proteomics 20190509 11


Protein posttranslational modifications critically regulate a range of physiological and disease processes. In addition to tyrosine, serine, and threonine phosphorylation, reversible N-ε acylation and alkylation of protein lysine residues also modulate diverse aspects of cellular function. Studies of lysine acyl and alkyl modifications have focused on nuclear proteins in epigenetic regulation; however, lysine modifications are also prevalent on cytosolic proteins to serve increasingly apparent,  ...[more]

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