Optimized filopodia formation requires myosin tail domain cooperation
| Autor: | Ashley L. Arthur, Fernanda Pires Borrega, Carlos Kikuti, Livia D. Songster, Anne Houdusse, Akash Bhattacharya, Margaret A. Titus, Helena Sirkia |
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| Přispěvatelé: | Compartimentation et dynamique cellulaires (CDC), Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), The University of Texas Health Science Center at Houston (UTHealth), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), University of Minnesota [Twin Cities] (UMN), University of Minnesota System |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Myosin tail
Protozoan Proteins macromolecular substances [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] Myosins Antiparallel (biochemistry) 03 medical and health sciences 0302 clinical medicine Protein Domains Myosin Dictyostelium Pseudopodia Actin ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences Multidisciplinary Chemistry Tail region Dimerization activity PNAS Plus Biophysics Protein Multimerization Filopodia 030217 neurology & neurosurgery Filopodia formation |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (44), pp.22196-22204. ⟨10.1073/pnas.1901527116⟩ |
| ISSN: | 0027-8424 1091-6490 |
| DOI: | 10.1073/pnas.1901527116⟩ |
| Popis: | Filopodia are actin-filled protrusions employed by cells to interact with their environment. Filopodia formation in Amoebozoa and Metazoa requires the phylogenetically diverse MyTH4-FERM (MF) myosins DdMyo7 and Myo10, respectively. While Myo10 is known to form antiparallel dimers, DdMyo7 lacks a coiled-coil domain in its proximal tail region, raising the question of how such divergent motors perform the same function. Here, it is shown that the DdMyo7 lever arm plays a role in both autoinhibition and function while the proximal tail region can mediate weak dimerization, and is proposed to be working in cooperation with the C-terminal MF domain to promote partner-mediated dimerization. Additionally, a forced dimer of the DdMyo7 motor is found to weakly rescue filopodia formation, further highlighting the importance of the C-terminal MF domain. Thus, weak dimerization activity of the DdMyo7 proximal tail allows for sensitive regulation of myosin activity to prevent inappropriate activation of filopodia formation. The results reveal that the principles of MF myosin-based filopodia formation are conserved via divergent mechanisms for dimerization. |
| Databáze: | OpenAIRE |
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