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Heuck, A. ; Du, T.G. ; Jellbauer, S.* ; Richter, K.* ; Kruse, C.* ; Jaklin, S. ; Müller, M. ; Buchner, J.* ; Jansen, R.P. ; Niessing, D.

Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes.

Proc. Natl. Acad. Sci. U.S.A. 105, 19778-19783 (2007)
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Myosin-motors are conserved from yeast to human and transport a great variety of cargoes. Most plus-end directed myosins, which constitute the vast majority of all myosin motors, form stable dimers and interact constitutively with their cargo complexes. To date, little is known about regulatory mechanisms for cargo-complex assembly. In this study, we show that the type V myosin Myo4p binds to its cargo via two distinct binding regions, the C-terminal tail and a coiled-coil domain-containing fragment. Furthermore, we find that Myo4p is strictly monomeric at physiologic concentrations. Because type V myosins are thought to require dimerization for processive movement, a mechanism must be in place to ensure that oligomeric Myo4p is incorporated into cargo-translocation complexes. Indeed, we find that artificial dimerization of the Myo4p C-terminal tail promotes stabilization of myosin-cargo complexes, suggesting that full-length Myo4p dimerizes in the cocomplex as well. We also combined the Myo4p C-terminal tail with the coiled-coil region, lever arm, and motor domain from a different myosin to form constitutively dimeric motor proteins. This heterologous motor successfully translocates its cargo in vivo, suggesting that wild-type Myo4p may also function as a dimer during cargo-complex transport.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter cell asymmetry; Myo4p; RNA localization; She3p; motor protein; ASH1 MESSENGER-RNA; BUDDING YEAST DEPENDS; SACCHAROMYCES-CEREVISIAE; LOCALIZATION ELEMENTS; PROTEIN; MYO4P; TRANSPORT; BUD; MOTOR; SHE2P
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Quellenangaben Band: 105, Heft: 50, Seiten: 19778-19783 Artikelnummer: , Supplement: ,
Verlag National Academy of Sciences
Begutachtungsstatus Peer reviewed