| Structural highlights
Function
[MYO4_YEAST] Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruited to specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease, via its interaction with SHE3.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Type V myosin (MyoV)-dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2-tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail-lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain.
The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.,Heuck A, Fetka I, Brewer DN, Huls D, Munson M, Jansen RP, Niessing D J Cell Biol. 2010 May 3;189(3):497-510. PMID:20439999[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Munchow S, Sauter C, Jansen RP. Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins. J Cell Sci. 1999 May;112 ( Pt 10):1511-8. PMID:10212145
- ↑ Bohl F, Kruse C, Frank A, Ferring D, Jansen RP. She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p. EMBO J. 2000 Oct 16;19(20):5514-24. PMID:11032818 doi:http://dx.doi.org/10.1093/emboj/19.20.5514
- ↑ Long RM, Gu W, Lorimer E, Singer RH, Chartrand P. She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. EMBO J. 2000 Dec 1;19(23):6592-601. PMID:11101531 doi:http://dx.doi.org/10.1093/emboj/19.23.6592
- ↑ Kruse C, Jaedicke A, Beaudouin J, Bohl F, Ferring D, Guttler T, Ellenberg J, Jansen RP. Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p. J Cell Biol. 2002 Dec 23;159(6):971-82. Epub 2002 Dec 23. PMID:12499354 doi:http://dx.doi.org/10.1083/jcb.200207101
- ↑ Gonsalvez GB, Little JL, Long RM. ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex. J Biol Chem. 2004 Oct 29;279(44):46286-94. Epub 2004 Aug 23. PMID:15328357 doi:http://dx.doi.org/10.1074/jbc.M406086200
- ↑ Heuck A, Fetka I, Brewer DN, Huls D, Munson M, Jansen RP, Niessing D. The structure of the Myo4p globular tail and its function in ASH1 mRNA localization. J Cell Biol. 2010 May 3;189(3):497-510. PMID:20439999 doi:10.1083/jcb.201002076
- ↑ Heuck A, Fetka I, Brewer DN, Huls D, Munson M, Jansen RP, Niessing D. The structure of the Myo4p globular tail and its function in ASH1 mRNA localization. J Cell Biol. 2010 May 3;189(3):497-510. PMID:20439999 doi:10.1083/jcb.201002076
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