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Published 23 December 2002. doi:10.1083/jcb.200207101
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© The Rockefeller University Press, 0021-9525/2002/12/971 $5.00
The Journal of Cell Biology, Volume 159, Number 6, 971-982

Article

Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p



Claudia Kruse1, Andreas Jaedicke1, Joël Beaudouin2, Florian Böhl1, Dunja Ferring1, Thomas Güttler1, Jan Ellenberg2 and Ralf-Peter Jansen1

1 Zentrum für Molekulare Biologie, Universität Heidelberg, D-69120 Heidelberg, Germany
2 Gene Expression and Cell Biology/Biophysics Programs, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany

Address correspondence to Ralf-Peter Jansen, ZMBH, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany. Tel.: 49-6221-546869. Fax: 49-6221-545892. E-mail: r.jansen{at}zmbh.uni-heidelberg.de

Class V myosins are motor proteins with functions in vesicle transport, organelle segregation, and RNA localization. Although they have been extensively studied, only little is known about the regulation of their spatial distribution. Here we demonstrate that a GFP fusion protein of the budding yeast class V myosin Myo4p accumulates at the bud cortex and is a component of highly dynamic cortical particles. Bud-specific enrichment depends on Myo4p's association with its cargo, a ribonucleoprotein complex containing the RNA-binding protein She2p. Cortical accumulation of Myo4p at the bud tip can be explained by a transient retention mechanism that requires SHE2 and, apparently, localized mRNAs bound to She2p. A mutant She2 protein that is unable to recognize its cognate target mRNA, ASH1, fails to localize Myo4p. Mutant She2p accumulates inside the nucleus, indicating that She2p shuttles between the nucleus and cytoplasm and is exported in an RNA-dependent manner. Consistently, inhibition of nuclear mRNA export results in nuclear accumulation of She2p and cytoplasmic Myo4p mislocalization. Loss of She2p can be complemented by direct targeting of a heterologous lacZ mRNA to a complex of Myo4p and its associated adaptor She3p, suggesting that She2p's function in Myo4p targeting is to link an mRNA to the motor complex.

Key Words: myosin-V; RNA localization; FLIP; myosin regulation; ASH1


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