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A systematic screening pipeline identifies a new regulator of tyrosinated microtubule dynamics

ABSTRACT: Tubulin detyrosination is a reversible post-translational modification thought to be important for processes including the generation of cell polarity and cell division. The Y/ΔY cycle does not affect the intrinsic properties of microtubules per se, but rather influences the cohort of microtubule-associated proteins (MAPs) and motor proteins that associate with microtubules. Here we present a screening pipeline to identify proteins that bind microtubules in a manner that depends on the Y versus ΔY state.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sarah Haynes

LAB HEAD: Alexey Nesvizhskii

PROVIDER: PXD030448 | Pride | 2022-08-16

REPOSITORIES: Pride

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EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules.

Hotta Takashi T McAlear Thomas S TS Yue Yang Y Higaki Takumi T Haynes Sarah E SE Nesvizhskii Alexey I AI Sept David D Verhey Kristen J KJ Bechstedt Susanne S Ohi Ryoma R

Current biology : CB 20220812 18

Tubulin post-translational modifications (PTMs) alter microtubule properties by affecting the binding of microtubule-associated proteins (MAPs). Microtubule detyrosination, which occurs by proteolytic removal of the C-terminal tyrosine from ɑ-tubulin, generates the oldest known tubulin PTM, but we lack comprehensive knowledge of MAPs that are regulated by this PTM. We developed a screening pipeline to identify proteins that discriminate between Y- and ΔY-microtubules and found that echinoderm mi ...[more]

PMID: 35963242

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