Luke M. McAloon

ORCID: 0000-0002-9646-5544
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About
Contact & Profiles
Research Areas
  • Protein Kinase Regulation and GTPase Signaling
  • Metabolism, Diabetes, and Cancer
  • Pancreatic function and diabetes
  • Ion channel regulation and function
  • Genetics and Neurodevelopmental Disorders
  • 14-3-3 protein interactions
  • Diet and metabolism studies
  • PI3K/AKT/mTOR signaling in cancer
  • Cellular transport and secretion
  • Calcium signaling and nucleotide metabolism
  • Apelin-related biomedical research
  • Receptor Mechanisms and Signaling
  • Amino Acid Enzymes and Metabolism
  • Adipose Tissue and Metabolism
  • Ubiquitin and proteasome pathways
  • Bipolar Disorder and Treatment

St Vincents Institute of Medical Research
2020-2025

Australian Catholic University
2021-2025

Monash University
2025

The University of Melbourne
2020

Protein Serine Kinase H1 (PSKH1) was recently identified as a crucial factor in kidney development and is overexpressed prostate, lung, cancers. However, little known about PSKH1 regulatory mechanisms, leading to its classification “dark” kinase. Here, we used biochemistry mass spectrometry define PSKH1’s consensus substrate motif, protein interactors, how including Ca 2+ sensor proteins, promote or suppress activity. Intriguingly, despite the absence of canonical Calmodulin binding...

10.1073/pnas.2420961122 article EN cc-by Proceedings of the National Academy of Sciences 2025-02-18

The nutrient-sensitive protein kinases AMPK and mTORC1 form a fundamental negative feedback loop that governs cell growth proliferation. phosphorylates α2-S345 in the αβγ heterotrimer to suppress its activity promote proliferation under nutrient stress conditions. Whether contains other functional substrates is unknown. Using mass spectrometry, we generated precise stoichiometry profiles of phosphorylation sites across all twelve complexes expressed proliferating human cells identified seven...

10.1038/s44324-025-00052-7 article EN cc-by npj Metabolic Health and Disease 2025-03-04

The calcium-calmodulin–dependent protein kinase kinase-2 (CaMKK2) is a key regulator of cellular and whole-body energy metabolism. It known to be activated by increases in intracellular Ca2+, but the mechanisms which it inactivated are less clear. CaMKK2 inhibition protects against prostate cancer, hepatocellular carcinoma, metabolic derangements induced high-fat diet; therefore, elucidating that inactivate has important therapeutic implications. Here we show stimulation cAMP-dependent A...

10.1074/jbc.ra120.013756 article EN cc-by Journal of Biological Chemistry 2020-09-10

AMP-activated protein kinase (AMPK) is a master regulator of cellular energy homeostasis and therapeutic target for metabolic diseases. Co/post-translational N-myristoylation glycine-2 (Gly2) the AMPK β subunit has been suggested to regulate distribution between cytosol membranes through "myristoyl switch" mechanism. However, relevance myristoylation signaling in cells vivo unclear. Here, we generated knockin mice with Gly2-to-alanine point mutation AMPKβ1 (β1-G2A). We demonstrate that...

10.1016/j.celrep.2022.111862 article EN cc-by-nc-nd Cell Reports 2022-12-01

Abstract Protein Serine Kinase H1 (PSKH1) was recently identified as a crucial factor in kidney development and is overexpressed prostate, lung cancers. However, little known about PSKH1 regulatory mechanisms, leading to its classification “dark” kinase. Here, we used biochemistry mass spectrometry define PSKH1’s consensus substrate motif, protein interactors, how including Ca 2+ sensor proteins, promote or suppress activity. Intriguingly, despite the absence of canonical Calmodulin binding...

10.1101/2024.10.20.619163 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-10-22
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