2. Academic Validation
  3. SILAC kinase screen identifies potential MASTL substrates

SILAC kinase screen identifies potential MASTL substrates

  • Sci Rep. 2022 Jun 22;12(1):10568. doi: 10.1038/s41598-022-14933-0.
Kamila A Marzec  # 1,  Samuel Rogers  # 2,  Rachael McCloy 3,  Benjamin L Parker 4,  David E James 5 6,  D Neil Watkins 7 8,  Andrew Burgess 9 10
Affiliations

Affiliations

  • 1 ANZAC Research Institute, Concord Hospital, Concord, NSW, 2139, Australia.
  • 2 Children's Medical Research Institute, The University of Sydney, Westmead, Australia.
  • 3 The Kinghorn Cancer Centre, Garvan Institute of Medical Research, Sydney, NSW, 2010, Australia.
  • 4 Department of Anatomy and Physiology, University of Melbourne, Melbourne, VIC, 3010, Australia.
  • 5 Charles Perkins Centre, School of Life and Environmental Sciences, The University of Sydney, Sydney, NSW, 2006, Australia.
  • 6 School of Medical Sciences, The University of Sydney, Sydney, NSW, 2006, Australia.
  • 7 Department of Internal Medicine, Rady Faculty of Health Sciences, University of Manitoba, Winnipeg, MB, R3E 0W2, Canada.
  • 8 CancerCare Manitoba Research Institute, Winnipeg, MB, R3E-0V9, Canada.
  • 9 ANZAC Research Institute, Concord Hospital, Concord, NSW, 2139, Australia. andrew.burgess1@health.nsw.gov.au.
  • 10 The University of Sydney Concord Clinical School, Faculty of Medicine and Health, Sydney, NSW, 2139, Australia. andrew.burgess1@health.nsw.gov.au.
  • # Contributed equally.
PMID: 35732702 DOI: 10.1038/s41598-022-14933-0
Abstract

Microtubule-associated serine/threonine kinase-like (MASTL) has emerged as a critical regulator of mitosis and as a potential oncogene in a variety of Cancer types. To date, Arpp-19/ENSA are the only known substrates of MASTL. However, with the roles of MASTL expanding and increased interest in development of MASTL inhibitors, it has become critical to determine if there are additional substrates and what the optimal consensus motif for MASTL is. Here we utilized a whole cell lysate in vitro kinase screen combined with stable isotope labelling of Amino acids in Cell Culture (SILAC) to identify potential substrates and the residue preference of MASTL. Using the related AGC kinase family members Akt1/2, the kinase screen identified several known and new substrates highly enriched for the validated consensus motif of Akt. Applying this method to MASTL identified 59 phospho-sites on 67 proteins that increased in the presence of active MASTL. Subsequent in vitro kinase assays suggested that MASTL may phosphorylate hnRNPM, YB1 and TUBA1C under certain in vitro conditions. Taken together, these data suggest that MASTL may phosphorylate several additional substrates, providing insight into the ever-increasing biological functions and roles MASTL plays in driving Cancer progression and therapy resistance.

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