Proteopedia

6ixp

Structure of Myo2-GTD in complex with Mmr1Structure of Myo2-GTD in complex with Mmr1

Structural highlights

6ixp is a 6 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.733Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYO2_YEAST Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.[1] [2] [3] [4] [5] [6] [7] [8]

Publication Abstract from PubMed

Class V myosins are actin-dependent motors, which recognize numerous cellular cargos mainly via the C-terminal globular tail domain (GTD). Myo2, a yeast class V myosin, can transport a broad range of organelles. However, little is known about the capacity of Myo2-GTD to recognize such a diverse array of cargos specifically at the molecular level. Here, we solved crystal structures of Myo2-GTD (at 1.9-3.1 A resolutions) in complex with three cargo adaptor proteins: Smy1 (for polarization of secretory vesicles), Inp2 (for peroxisome transport), and Mmr1 (for mitochondria transport). The structures of Smy1- and Inp2-bound Myo2-GTD, along with site-directed mutagenesis experiments, revealed a binding site in subdomain-I having a hydrophobic groove with high flexibility enabling Myo2-GTD to accommodate different protein sequences. The Myo2-GTD-Mmr1 complex structure confirmed and complemented a previously identified mitochondrion/vacuole-specific binding region. Moreover, differences between the conformations and locations of cargo-binding sites identified here for Myo2 and those reported for mammalian MyoVA (MyoVA) suggest that class V myosins potentially have co-evolved with their specific cargos. Our structural and biochemical analysis not only uncovers a molecular mechanism that explains the diverse cargo recognition by Myo2-GTD, but also provides structural information useful for future functional studies of class V myosins in cargo transport.

Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.,Tang K, Li Y, Yu C, Wei Z J Biol Chem. 2019 Apr 12;294(15):5896-5906. doi: 10.1074/jbc.RA119.007550. Epub, 2019 Feb 25. PMID:30804213[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Catlett NL, Duex JE, Tang F, Weisman LS. Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes. J Cell Biol. 2000 Aug 7;150(3):513-26. PMID:10931864
  2. ↑ Rossanese OW, Reinke CA, Bevis BJ, Hammond AT, Sears IB, O'Connor J, Glick BS. A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J Cell Biol. 2001 Apr 2;153(1):47-62. PMID:11285273
  3. ↑ Reck-Peterson SL, Tyska MJ, Novick PJ, Mooseker MS. The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors. J Cell Biol. 2001 May 28;153(5):1121-6. PMID:11381095
  4. ↑ Hoepfner D, van den Berg M, Philippsen P, Tabak HF, Hettema EH. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J Cell Biol. 2001 Dec 10;155(6):979-90. Epub 2001 Dec 3. PMID:11733545 doi:http://dx.doi.org/10.1083/jcb.200107028
  5. ↑ Schott DH, Collins RN, Bretscher A. Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length. J Cell Biol. 2002 Jan 7;156(1):35-9. Epub 2002 Jan 7. PMID:11781333 doi:http://dx.doi.org/10.1083/jcb.200110086
  6. ↑ Itoh T, Watabe A, Toh-E A, Matsui Y. Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae. Mol Cell Biol. 2002 Nov;22(22):7744-57. PMID:12391144
  7. ↑ Hwang E, Kusch J, Barral Y, Huffaker TC. Spindle orientation in Saccharomyces cerevisiae depends on the transport of microtubule ends along polarized actin cables. J Cell Biol. 2003 May 12;161(3):483-8. PMID:12743102 doi:http://dx.doi.org/10.1083/jcb.200302030
  8. ↑ Rossi G, Brennwald P. Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis. Mol Biol Cell. 2011 Mar 15;22(6):842-57. doi: 10.1091/mbc.E10-07-0570. Epub 2011 , Jan 19. PMID:21248204 doi:http://dx.doi.org/10.1091/mbc.E10-07-0570
  9. ↑ Tang K, Li Y, Yu C, Wei Z. Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2. J Biol Chem. 2019 Apr 12;294(15):5896-5906. doi: 10.1074/jbc.RA119.007550. Epub, 2019 Feb 25. PMID:30804213 doi:http://dx.doi.org/10.1074/jbc.RA119.007550

6ixp, resolution 2.73Å

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