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Título: | Kidins220/ARMS modulates the activity of microtubule-regulating proteins and controls neuronal polarity and development |
Autor: | Higuero, Alonso M. CSIC ORCID; Sánchez-Ruiloba, Lucía CSIC ORCID; García del Portillo, Francisco CSIC ORCID ; Iglesias, Teresa CSIC ORCID | Fecha de publicación: | 2010 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 285(2): 1343-1357 (2010) | Resumen: | In order for neurons to perform their function, they must establish a highly polarized morphology characterized, in most of the cases, by a single axon and multiple dendrites. Herein we find that the evolutionarily conserved protein Kidins220 (kinase D-interacting substrate of 220-kDa), also known as ARMS (ankyrin repeat-rich membrane spanning), a downstream effector of protein kinase D and neurotrophin and ephrin receptors, regulates the establishment of neuronal polarity and development of dendrites. Kidins220/ARMS gain and loss of function experiments render severe phenotypic changes in the processes extended by hippocampal neurons in culture. Although Kidins220/ARMS early overexpression hinders neuronal development, its down-regulation by RNA interference results in the appearance of multiple longer axon-like extensions as well as aberrant dendritic arbors. We also find that Kidins220/ARMS interacts with tubulin and microtubule-regulating molecules whose role in neuronal morphogenesis is well established (microtubule-associated proteins 1b, 1a, and 2 and two members of the stathmin family). Importantly, neurons where Kidins220/ARMS has been knocked down register changes in the phosphorylation activity of MAP1b and stathmins. Altogether, our results indicate that Kidins220/ARMS is a key modulator of the activity of microtubule-regulating proteins known to actively regulate neuronal morphogenesis and suggest a mechanism by which it contributes to control neuronal development. | URI: | http://hdl.handle.net/10261/77260 | DOI: | 10.1074/jbc.M109.024703 | Identificadores: | doi: 10.1074/jbc.M109.024703 issn: 0021-9258 e-issn: 1083-351X |
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