MARK3 phosphorylates MITF-M on S173

Stable Identifier
R-HSA-9926483
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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MARK3, also known as C-TAK1, phosphorylates cytosolic MITF-M, promoting the interaction of MITF-M with 14-3-3 proteins that function to retain it in the cytosol. MARK3-dependent phosphorylation is inhibited by treatment of cells with CSF (colony stimulating factor) and RANKL (receptor activator of nuclear factor kappa beta ligand), disrupting the interaction with 14-3-3 dimers and promoting nuclear localization of MITF-M (Bornisz et al, 2006). CSF and RANKL are produced by osteoblasts and are required for osteoclast formation (reviewed in Boyle et al, 2003).
Literature References
PubMed ID Title Journal Year
16822840 Microphthalmia-associated transcription factor interactions with 14-3-3 modulate differentiation of committed myeloid precursors

Bronisz, A, Sharma, SM, Hu, R, Godlewski, J, Tzivion, G, Mansky, KC, Ostrowski, MC

Mol Biol Cell 2006
12748652 Osteoclast differentiation and activation

Boyle, WJ, Simonet, WS, Lacey, DL

Nature 2003
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Catalyst Activity

protein serine/threonine kinase activity of MARK3 [cytosol]

This event is regulated
Orthologous Events
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