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First published online October 7, 2009
doi: 10.1242/10.1242/jcs.050344

Journal of Cell Science 122, 3810-3821 (2009)
Published by The Company of Biologists 2009
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Research Article

Myosin-Va-interacting protein, RILPL2, controls cell shape and neuronal morphogenesis via Rac signaling

Marie-France Lisé1,2,*, Deepak P. Srivastava3,{ddagger}, Pamela Arstikaitis1,{ddagger}, Robyn L. Lett2, Razan Sheta1, Vijay Viswanathan1, Peter Penzes3, Timothy P. O'Connor2,* and Alaa El-Husseini1,§

1 Department of Psychiatry and Brain Research Center, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3
2 Cellular and Physiological Sciences, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3
3 Department of Physiology, Northwestern University, Feinberg School of Medicine, Chicago, IL 60611, USA

* Authors for correspondence (marief.lise{at}gmail.com; jimo{at}interchange.ubc.ca)

Accepted 13 August 2009

Neuronal morphology plays an essential role in neuronal function. The establishment and maintenance of neuronal morphology is intimately linked to the actin cytoskeleton; however, the molecular mechanisms that regulate changes in neuronal morphology are poorly understood. Here we identify a novel myosin-Va (MyoVa)-interacting protein, RILPL2, which regulates cellular morphology. Overexpression of this protein in young or mature hippocampal neurons results in an increase in the number of spine-like protrusions. By contrast, knockdown of endogenous RILPL2 in neurons by short hairpin RNA (shRNA) interference results in reduced spine-like protrusions, a phenotype rescued by overexpression of an shRNA-insensitive RILPL2 mutant, suggesting a role for RILPL2 in both the establishment and maintenance of dendritic spines. Interestingly, we demonstrate that RILPL2 and the Rho GTPase Rac1 form a complex, and that RILPL2 is able to induce activation of Rac1 and its target, p21-activated kinase (Pak). Notably, both RILPL2-mediated morphological changes and activation of Rac1-Pak signaling were blocked by expression of a truncated tail form of MyoVa or MyoVa shRNA, demonstrating that MyoVa is crucial for proper RILPL2 function. This might represent a novel mechanism linking RILPL2, the motor protein MyoVa and Rac1 with neuronal structure and function.

Key words: RILPL2, Myosin-V, Rac1, Actin, Dendritic spine


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