Journal
NATURE CELL BIOLOGY
Volume 11, Issue 10, Pages 1191-U55Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1961
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Funding
- Biotechnology and Biological Science Research Council [BB/C514307/1]
- MRC [G9403619]
- MRC [G9403619, G0801865] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/C514307/1] Funding Source: researchfish
- Medical Research Council [G0801865, G9403619] Funding Source: researchfish
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The tumour suppressor PTEN can inhibit cell proliferation and migration as well as control cell growth, in different cell types(1). PTEN functions predominately as a lipid phosphatase, converting PtdIns(3,4,5)P-3 to PtdIns(4,5)P-2, thereby antagonizing PI(3) K (phosphoinositide 3-kinase) and its established downstream effector pathways(2). However, much is unclear concerning the mechanisms that regulate PTEN movement to the cell membrane, which is necessary for its activity towards PtdIns(3,4,5)P-3 (refs 3-5). Here we show a requirement for functional motor proteins in the control of PI3K signalling, involving a previously unknown association between PTEN and myosinV. FRET (Forster resonance energy transfer) measurements revealed that PTEN interacts directly with myosinV, which is dependent on PTEN phosphorylation mediated by CK2 and/or GSK3. Inactivation of myosinV transport function in neurons increased cell size, which, in line with known attributes of PTEN-loss(6,7), required PI(3) K and mTor. Our data demonstrate a myosin-based transport mechanism that regulates PTEN function, providing new insights into the signalling networks regulating cell growth.
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