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LUZP1 and the tumor suppressor EPLIN modulate actin stability to restrict primary cilia formation.

Authors
  • Gonçalves, João1
  • Sharma, Amit1
  • Coyaud, Étienne2
  • Laurent, Estelle M N2
  • Raught, Brian2, 3
  • Pelletier, Laurence1, 4
  • 1 Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. , (Canada)
  • 2 Princess Margaret Cancer Centre, University Health Network, Toronto, Ontario, Canada. , (Canada)
  • 3 Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada. , (Canada)
  • 4 Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada. , (Canada)
Type
Published Article
Journal
The Journal of Cell Biology
Publisher
The Rockefeller University Press
Publication Date
Jul 06, 2020
Volume
219
Issue
7
Identifiers
DOI: 10.1083/jcb.201908132
PMID: 32496561
Source
Medline
Language
English
License
Unknown

Abstract

Cilia and flagella are microtubule-based cellular projections with important sensory and motility functions. Their absence or malfunction is associated with a growing number of human diseases collectively referred to as ciliopathies. However, the fundamental mechanisms underpinning cilia biogenesis and functions remain only partly understood. Here, we show that depleting LUZP1 or its interacting protein, EPLIN, increases the levels of MyosinVa at the centrosome and primary cilia formation. We further show that LUZP1 localizes to both actin filaments and the centrosome/basal body. Like EPLIN, LUZP1 is an actin-stabilizing protein that regulates actin dynamics, at least in part, by mobilizing ARP2 to the centrosomes. Both LUZP1 and EPLIN interact with known ciliogenesis and cilia-length regulators and as such represent novel players in actin-dependent centrosome to basal body conversion. Ciliogenesis deregulation caused by LUZP1 or EPLIN loss may thus contribute to the pathology of their associated disease states. © 2020 Gonçalves et al.

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