biostudies-literatureUnknown44Fathima I<h4>Background</h4>MAST2 (Microtubule-Associated Serine/Threonine Kinase 2) is an enigmatic serine/threonine kinase that is considered to bridge microtubule-associated cytoskeletal architecture through its phospho-regulatory networks. Yet, MAST2 remains a dark horse in the human kinome, as the molecular details on its structure, upstream regulators, and downstream phosphorylation targets remain unknown.<h4>Methods and results</h4>To interpret MAST2-linked phospho-signaling dynamics, PubMed-indexed articles were curated based on predefined MeSH terms to obtain global cellular phosphoproteomics datasets. Among 105 class I phosphosites in MAST2 identified across cellular phosphoproteomics datasets, 2 phosphosites, S74 and S148, were represented more abundantly compared to other phosphosites, Biochemistry and biophysics reports102277https://www.ebi.ac.uk/biostudies/studies/S-EPMC12489769biostudies-literatureCellular phospho-signaling map of the enigmatic serine/threonine kinase MAST2.PMC12489769Nishana APriyanka PNaurah Vattoth NPerunelly Gopalakrishnan AFathima IMahin ARaju RSoman SfalseCellular phospho-signaling map of the enigmatic serine/threonine kinase MAST2.<h4>Background</h4>MAST2 (Microtubule-Associated Serine/Threonine Kinase 2) is an enigmatic serine/threonine kinase that is considered to bridge microtubule-associated cytoskeletal architecture through its phospho-regulatory networks. Yet, MAST2 remains a dark horse in the human kinome, as the molecular details on its structure, upstream regulators, and downstream phosphorylation targets remain unknown.<h4>Methods and results</h4>To interpret MAST2-linked phospho-signaling dynamics, PubMed-indexed articles were curated based on predefined MeSH terms to obtain global cellular phosphoproteomics datasets. Among 105 class I phosphosites in MAST2 identified across cellular phosphoproteomics datasets, 2 phosphosites, S74 and S148, were represented more abundantly compared to other phosphosites, 2025-01-01T00:00:00Z2025 Dec2026-06-01T03:15:42.096Z2026-06-01T03:06:26.836ZS-EPMC124897694104912610.1016/j.bbrep.2025.102277