Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment

Collectively, these findings establish a phosphoinositide- and cytoskeleton-guided mechanism that governs myosin-1 isoform-specific functions, providing new insights into how motor proteins interpret complex lipid and cytoskeletal cues to regulate membrane remodelling and cytoskeletal dynamics across cellular states.

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Publication Details

Journal
Cell Communication and Signaling
Published
2025-12-04
DOI
https://doi.org/10.1186/s12964-025-02528-x
Primary Topic
Cardiomyopathy and Myosin Studies
Type
article
Field-Weighted Citation Impact
0.00
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article

Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment

Girish Rajendraprasad, Georgios Tsiavaliaris, Petra Uta, Almke Bader et al.
Cell Communication and Signaling
Cardiomyopathy and Myosin Studies
article

Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment

Girish Rajendraprasad, Georgios Tsiavaliaris, Petra Uta, Almke Bader, Muriel Erent, Peter Franz, Matthias Preller, Tim Scholz, Despoina Kyriazi
article en

Abstract

Collectively, these findings establish a phosphoinositide- and cytoskeleton-guided mechanism that governs myosin-1 isoform-specific functions, providing new insights into how motor proteins interpret complex lipid and cytoskeletal cues to regulate membrane remodelling and cytoskeletal dynamics across cellular states.

Cell Communication and SignalingVol. 23(1)
Hochschule Bonn-Rhein-Sieg (DE), Medizinische Hochschule Hannover (DE), University of Warwick (GB)
Openalex Percentile: Top 45%
Cardiomyopathy and Myosin Studies
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