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Protrudin Induces Neurite Formation by Directional Membrane Trafficking
Abstract
Guanosine triphosphatases of the Rab family are key regulators of membrane trafficking, with Rab11 playing a specific role in membrane recycling. We identified a mammalian protein, protrudin, that promoted neurite formation through interaction with the guanosine diphosphate (GDP)–bound form of Rab11. Phosphorylation of protrudin by extracellular signal–regulated kinase (ERK) in response to nerve growth factor promoted protrudin association with Rab11-GDP. Down-regulation of protrudin by RNA interference induced membrane extension in all directions and inhibited neurite formation. Thus, protrudin regulates Rab11-dependent membrane recycling to promote the directional membrane trafficking required for neurite formation.
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Citations
Cited by
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Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413
Role of Rab GTPases in Membrane Traffic and Cell Physiology
Hutagalung, A. H., & Novick, P. J. (2011) · Physiological Reviews · doi:10.1152/physrev.00059.2009 · Cited by 1,460
Repeated ER–endosome contacts promote endosome translocation and neurite outgrowth
Raiborg, C., Wenzel, E. M., Pedersen, N. M., Olsvik, H., Schink, K. O., Schultz, S. W., Vietri, M., Nisi, V., Bucci, C., Brech, A., et al. (2015) · Nature · doi:10.1038/nature14359 · Cited by 414
Cellular functions of Rab GTPases at a glance
Zhen, Y., & Stenmark, H. (2015) · Journal of Cell Science · doi:10.1242/jcs.166074 · Cited by 400
Hereditary spastic paraplegia: Clinical-genetic characteristics and evolving molecular mechanisms
Lo Giudice, T., Lombardi, F., Santorelli, F. M., Kawarai, T., & Orlacchio, A. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.06.011 · Cited by 347
Metadata
- Authors
- Shirane, M., & Nakayama, K. I.
- Venue
- Science
- Published
- 2006-11-03
- Volume
- 314
- Issue
- 5800
- Pages
- 818-821
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2011005136
- Cited by
- 197
- References
- 0
- FWCI
- 4.74
- Type
- journal article
- Language
- en
- Open access
- closed
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