Endocytic myosin-1 is a force-insensitive, power-generating motor
Myosins are required for clathrin-mediated endocytosis, but their precise molecular roles in this process are not known. This is, in part, because the biophysical properties of the relevant motors have not been investigated. Myosins have diverse mechanochemical activities, ranging from powerful cont...
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| Veröffentlicht in: | The Journal of cell biology 2023-10, Vol.222 (10), p.1 |
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| creator | Pedersen, Ross T A Snoberger, Aaron Pyrpassopoulos, Serapion Safer, Daniel Drubin, David G Ostap, E Michael |
| description | Myosins are required for clathrin-mediated endocytosis, but their precise molecular roles in this process are not known. This is, in part, because the biophysical properties of the relevant motors have not been investigated. Myosins have diverse mechanochemical activities, ranging from powerful contractility against mechanical loads to force-sensitive anchoring. To better understand the essential molecular contribution of myosin to endocytosis, we studied the in vitro force-dependent kinetics of the Saccharomyces cerevisiae endocytic type I myosin called Myo5, a motor whose role in clathrin-mediated endocytosis has been meticulously studied in vivo. We report that Myo5 is a low-duty-ratio motor that is activated ∼10-fold by phosphorylation and that its working stroke and actin-detachment kinetics are relatively force-insensitive. Strikingly, the in vitro mechanochemistry of Myo5 is more like that of cardiac myosin than that of slow anchoring myosin-1s found on endosomal membranes. We, therefore, propose that Myo5 generates power to augment actin assembly-based forces during endocytosis in cells. |
| doi_str_mv | 10.1083/jcb.202303095 |
| format | Article |
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This is, in part, because the biophysical properties of the relevant motors have not been investigated. Myosins have diverse mechanochemical activities, ranging from powerful contractility against mechanical loads to force-sensitive anchoring. To better understand the essential molecular contribution of myosin to endocytosis, we studied the in vitro force-dependent kinetics of the Saccharomyces cerevisiae endocytic type I myosin called Myo5, a motor whose role in clathrin-mediated endocytosis has been meticulously studied in vivo. We report that Myo5 is a low-duty-ratio motor that is activated ∼10-fold by phosphorylation and that its working stroke and actin-detachment kinetics are relatively force-insensitive. Strikingly, the in vitro mechanochemistry of Myo5 is more like that of cardiac myosin than that of slow anchoring myosin-1s found on endosomal membranes. We, therefore, propose that Myo5 generates power to augment actin assembly-based forces during endocytosis in cells.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.202303095</identifier><identifier>PMID: 37549220</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Actin ; Actins ; Biochemistry ; Biophysics ; Clathrin ; Cytoskeleton ; Endocytosis ; Kinetics ; Muscle contraction ; Myosin ; Myosin Type I - genetics ; Myosins - genetics ; Phosphorylation ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins - genetics ; Trafficking</subject><ispartof>The Journal of cell biology, 2023-10, Vol.222 (10), p.1</ispartof><rights>2023 Pedersen et al.</rights><rights>Copyright Rockefeller University Press Oct 2023</rights><rights>2023 Pedersen et al. 2023 Pedersen et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c416t-47d17fe861105d0c04b0c7170af1be304c74358b828e5bf5dab1abd61e1d64e33</citedby><cites>FETCH-LOGICAL-c416t-47d17fe861105d0c04b0c7170af1be304c74358b828e5bf5dab1abd61e1d64e33</cites><orcidid>0000-0002-9728-9239 ; 0000-0002-0542-1424 ; 0000-0002-3890-3972 ; 0000-0003-0544-9360 ; 0000-0003-3002-6271 ; 0000-0001-9607-9312</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37549220$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pedersen, Ross T A</creatorcontrib><creatorcontrib>Snoberger, Aaron</creatorcontrib><creatorcontrib>Pyrpassopoulos, Serapion</creatorcontrib><creatorcontrib>Safer, Daniel</creatorcontrib><creatorcontrib>Drubin, David G</creatorcontrib><creatorcontrib>Ostap, E Michael</creatorcontrib><title>Endocytic myosin-1 is a force-insensitive, power-generating motor</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Myosins are required for clathrin-mediated endocytosis, but their precise molecular roles in this process are not known. 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| subjects | Actin Actins Biochemistry Biophysics Clathrin Cytoskeleton Endocytosis Kinetics Muscle contraction Myosin Myosin Type I - genetics Myosins - genetics Phosphorylation Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - genetics Trafficking |
| title | Endocytic myosin-1 is a force-insensitive, power-generating motor |
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