Data detailing the platelet acetyl-lysine proteome.

Area of Science:

• Biochemistry
• Proteomics
• Cell Biology

Background:

• Platelets play crucial roles in hemostasis and thrombosis.
• Protein lysine acetylation is a regulatory post-translational modification.
• Platelets, lacking nuclei, provide a unique model for studying cytosolic acetylation.

Purpose of the Study:

• To characterize the Nε-lysine acetylome of human blood platelets.
• To investigate the regulatory role of protein acetylation in platelet function.
• To explore acetylation of cytosolic proteins in an anucleate system.

Main Methods:

• Affinity purification coupled with mass spectrometry (AP-MS) was employed.
• Proteins undergoing Nε-lysine acetylation were identified in quiescent, washed human platelets.
• Proteomics data were deposited in the ProteomeXchange Consortium via PRIDE.

Main Results:

• A comprehensive dataset of acetyl-lysine modified proteins in platelets was generated.
• The data reveal potential acetylation-mediated regulatory pathways in platelet function.
• Identification of acetylated cytosolic proteins highlights their regulatory potential.

Conclusions:

• Protein lysine acetylation is a significant regulatory mechanism in human platelets.
• Platelets serve as a valuable model for studying cytosolic protein acetylation.
• The generated proteomics data provide a resource for further research into platelet biology and acetylation.