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Molecular and Cellular Biology, July 2009, p. 3623-3632, Vol. 29, No. 13
0270-7306/09/$08.00+0 doi:10.1128/MCB.00229-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
,
Leonard Rabinow,3
Guang-Chao Chen,1,2* and
Tzu-Ching Meng1,2*
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan,1 Institute of Biochemical Sciences, College of Life Sciences, National Taiwan University, Taipei, Taiwan,2 Signalisation Developpement et Cancer, Bat. 442 bis, Université Paris 11, CNRS UMR C8080, 91400 Orsay, France3
Received 20 February 2009/ Returned for modification 6 April 2009/ Accepted 18 April 2009
We identify Kette, a key regulator of actin polymerization, as a substrate for Drosophila protein tyrosine phosphatase PTP61F, as well as for dAbl tyrosine kinase. We further show that dAbl is a direct substrate for PTP61F. Therefore, Kette phosphotyrosine levels are regulated both directly and indirectly by PTP61F. Kette and PTP61F genetically interact in the regulation of F-actin organization in pupal eye discs, suggesting that tyrosine phosphorylation is essential for the proper regulation of Kette-mediated actin dynamics. This hypothesis was confirmed by demonstrating the loss of Kette-mediated F-actin organization and lamella formation in S2 cells in a Kette Y482F mutant in which the dAbl phosphorylation site was eliminated. Our results establish for the first time that PTP61F and dAbl ensure proper actin organization through the coordinated and reversible tyrosine phosphorylation of Kette.
Published ahead of print on 27 April 2009.
Supplemental material for this article may be found at http://mcb.asm.org/.
Present address: McGill Cancer Centre, McGill University, 3655 Sir William Osler Promenade, Cancer Pavilion, Montreal, Québec H3G 1Y6, Canada.
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