@article{RaymondCMerrittUriManorFelipeTSallesMhamedGratiAndreaCDoseWilliamCUnrathOmarAQuinteroChristopherMYengo2012,
  abstract = {Myosin IIIA (MYO3A) targets actin protrusion tips using a motility mechanism dependent on both motor and tail actin-binding activity [1]. We show that myosin IIIB (MYO3B) lacks tail actin-binding activity and is unable to target COS7 cell filopodia tips, yet is somehow able to target stereocilia tips. Strikingly, when MYO3B is coexpressed with espin-1 (ESPN1), a MYO3A cargo protein endogenously expressed in stereocilia [2], MYO3B targets and carries ESPN1 to COS7 filopodia tips. We show that this tip-localization is lost when we remove the ESPN1 C-terminus actin-binding site. We also demonstrate that, like MYO3A [2], MYO3B can elongate filopodia by transporting ESPN1 to the polymerizing end of actin filaments. The mutual dependence of MYO3B and ESPN1 for tip-localization reveals a novel mechanism for the cell to regulate myosin tip-localization via a reciprocal relationship with cargo that directly participates in actin binding for motility. Our results are consistent with a novel form of motility for class III myosins that requires both motor and tail domain actin-binding activity, and show that the actin-binding tail can be replaced by actin-binding cargo. This study also provides a framework to better understand the late-onset hearing loss phenotype in patients with MYO3A mutations. Go to:},
  author = {Merritt, Raymond C and Manor, Uri and Salles, Felipe T and Grati, M'hamed and Dose, Andrea C and Unrath, William C and Quintero, Omar A and Yengo, Christopher M and Kachar, Bechara},
  journal = {Current biology},
  number = {4},
  pages = {320--325},
  title = {{Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the tips of actin protrusions}},
  volume = {22},
  year = {2012}
}

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We also demonstrate that, like MYO3A [2], MYO3B can elongate filopodia by transporting ESPN1 to the polymerizing end of actin filaments. The mutual dependence of MYO3B and ESPN1 for tip-localization reveals a novel mechanism for the cell to regulate myosin tip-localization via a reciprocal relationship with cargo that directly participates in actin binding for motility. Our results are consistent with a novel form of motility for class III myosins that requires both motor and tail domain actin-binding activity, and show that the actin-binding tail can be replaced by actin-binding cargo. This study also provides a framework to better understand the late-onset hearing loss phenotype in patients with MYO3A mutations. Go to:","author":[{"propositions":[],"lastnames":["Merritt"],"firstnames":["Raymond","C"],"suffixes":[]},{"propositions":[],"lastnames":["Manor"],"firstnames":["Uri"],"suffixes":[]},{"propositions":[],"lastnames":["Salles"],"firstnames":["Felipe","T"],"suffixes":[]},{"propositions":[],"lastnames":["Grati"],"firstnames":["M'hamed"],"suffixes":[]},{"propositions":[],"lastnames":["Dose"],"firstnames":["Andrea","C"],"suffixes":[]},{"propositions":[],"lastnames":["Unrath"],"firstnames":["William","C"],"suffixes":[]},{"propositions":[],"lastnames":["Quintero"],"firstnames":["Omar","A"],"suffixes":[]},{"propositions":[],"lastnames":["Yengo"],"firstnames":["Christopher","M"],"suffixes":[]},{"propositions":[],"lastnames":["Kachar"],"firstnames":["Bechara"],"suffixes":[]}],"journal":"Current biology","number":"4","pages":"320–325","title":"Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the tips of actin protrusions","volume":"22","year":"2012","bibtex":"@article{RaymondCMerrittUriManorFelipeTSallesMhamedGratiAndreaCDoseWilliamCUnrathOmarAQuinteroChristopherMYengo2012,\r\n abstract = {Myosin IIIA (MYO3A) targets actin protrusion tips using a motility mechanism dependent on both motor and tail actin-binding activity [1]. We show that myosin IIIB (MYO3B) lacks tail actin-binding activity and is unable to target COS7 cell filopodia tips, yet is somehow able to target stereocilia tips. Strikingly, when MYO3B is coexpressed with espin-1 (ESPN1), a MYO3A cargo protein endogenously expressed in stereocilia [2], MYO3B targets and carries ESPN1 to COS7 filopodia tips. We show that this tip-localization is lost when we remove the ESPN1 C-terminus actin-binding site. We also demonstrate that, like MYO3A [2], MYO3B can elongate filopodia by transporting ESPN1 to the polymerizing end of actin filaments. The mutual dependence of MYO3B and ESPN1 for tip-localization reveals a novel mechanism for the cell to regulate myosin tip-localization via a reciprocal relationship with cargo that directly participates in actin binding for motility. Our results are consistent with a novel form of motility for class III myosins that requires both motor and tail domain actin-binding activity, and show that the actin-binding tail can be replaced by actin-binding cargo. This study also provides a framework to better understand the late-onset hearing loss phenotype in patients with MYO3A mutations. Go to:},\r\n author = {Merritt, Raymond C and Manor, Uri and Salles, Felipe T and Grati, M'hamed and Dose, Andrea C and Unrath, William C and Quintero, Omar A and Yengo, Christopher M and Kachar, Bechara},\r\n journal = {Current biology},\r\n number = {4},\r\n pages = {320--325},\r\n title = {{Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the tips of actin protrusions}},\r\n volume = {22},\r\n year = {2012}\r\n}\r\n\r\n","author_short":["Merritt, R. C","Manor, U.","Salles, F. T","Grati, M.","Dose, A. C","Unrath, W. C","Quintero, O. A","Yengo, C. M","Kachar, B."],"key":"RaymondCMerrittUriManorFelipeTSallesMhamedGratiAndreaCDoseWilliamCUnrathOmarAQuinteroChristopherMYengo2012","id":"RaymondCMerrittUriManorFelipeTSallesMhamedGratiAndreaCDoseWilliamCUnrathOmarAQuinteroChristopherMYengo2012","bibbaseid":"merritt-manor-salles-grati-dose-unrath-quintero-yengo-etal-myosiniiibusesanactinbindingmotifinitsespin1cargotoreachthetipsofactinprotrusions-2012","role":"author","urls":{},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://github.com/salkmanorlab/manor_publications/raw/main/manorlab_pubs.bib","dataSources":["edXsq84pNeYoA6wo6","dr3nCm3wyZkR7nFZf"],"keywords":[],"search_terms":["myosin","iiib","uses","actin","binding","motif","espin","cargo","reach","tips","actin","protrusions","merritt","manor","salles","grati","dose","unrath","quintero","yengo","kachar"],"title":"Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the tips of actin protrusions","year":2012}