Open AccessMICAL-L1 coordinates ciliogenesis by recruitment of EHD1 to the primary cilium
Author(s) -
Shuwei Xie,
Trey Farmer,
Naava Naslavsky,
Steve Caplan
Publication year - 2019
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.233973
Subject(s) - ciliogenesis , centrosome , basal body , cilium , biology , microbiology and biotechnology , centriole , microtubule , endocytic cycle , tubulin , genetics , flagellum , endocytosis , cell , gene , cell cycle
The endocytic protein, EHD1, plays an important role in ciliogenesis facilitating fusion of the ciliary vesicle and removal of CP110 from the mother centriole, as well as removal of Cep215 from centrioles to permit disengagement and duplication. However, the mechanism of its centrosomal recruitment remains unknown. Here we address the role of the EHD1 interaction partner, MICAL-L1, in ciliogenesis. MICAL-L1 knock-down impairs ciliogenesis similar to EHD1 knock-down, and MICAL-L1 localizes to cilia and centrosomes in ciliated and non-ciliated cells, respectively. Consistent with EHD1 function, MICAL-L1-depletion prevents CP110 removal from the mother centriole. Moreover, upon MICAL-L1-depletion EHD1 fails to localize to basal bodies. Since MICAL-L1 localizes to the centrosome even in non-ciliated cells, we hypothesized that it might be anchored to the centrosome via an interaction with centrosomal proteins. Using mass spectrometry, we identified several tubulins as potential MICAL-L1 interaction partners, and found a direct interaction between MICAL-L1 and both α/β-tubulins and γ-tubulin. Our data support the notion that a pool of centriolar γ-tubulin and/or α/β-tubulins anchor MICAL-L1 to the centriole, where it may recruit EHD1 to promote ciliogenesis.