STMND1 is A Phylogenetically Ancient Stathmin which Localizes to Motile Cilia and Exhibits Nuclear Translocation that Is Inhibited When Soluble Tubulin Concentration Increases
Mol Biol Cell. 2024 Apr 17:mbcE23120514. doi: 10.1091/mbc.E23-12-0514. Online ahead of print.ABSTRACTStathmins are small, unstructured proteins that bind tubulin dimers and are implicated in several human diseases, but whose function remains unknown. We characterized a new stathmin, STMND1 (Stathmin Domain Containing 1) as the human representative of an ancient sub-family. STMND1 features a N-terminal myristoylated and palmitoylated motif which directs it to membranes and a tubulin-binding stathmin-like domain (SLD) that contains an internal nuclear localization signal. Biochemistry and proximity labeling showed that STMND1 binds tubulin, and live imaging showed that tubulin binding inhibits translocation from cellular membranes to the nucleus. STMND1 is highly expressed in multiciliated epithelial cells, where it localizes to motile cilia. Overexpression in a model system increased the length of primary cilia. Our study suggests that the most ancient stathmins have cilium-related functions that involve sensing soluble tubulin. [Media: see text] [Media: see text].PMID:38630521 | DOI:10.1091/mbc.E23-12-0514
Source: Mol Biol Cell - Category: Molecular Biology Authors: Xiang Deng Bryan O Seguinot Gary Bradshaw Jong Suk Lee Shannon Coy Marian Kalocsay Sandro Santagata Timothy Mitchison Source Type: research