• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


Myosin V transports secretory vesicles via a Rab GTPase cascade and interaction with the exocyst complex.

Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to transport via direct interaction between Ypt31/32 and the yeast myosin V, Myo2. Here we show that Myo2 interacts directly with Sec4 and the exocyst subunit Sec15. Disruption of these interactions results in compromised growth and the accumulation of secretory vesicles. We identified the Sec15-binding region on Myo2 and also identified residues on Sec15 required for interaction with Myo2. That Myo2 interacts with Sec15 uncovers additional roles for the exocyst as an adaptor for molecular motors and implies similar roles for structurally related tethering complexes. Moreover, these studies predict that for many pathways, molecular motors attach to vesicles prior to their formation and remain attached until fusion.

Pubmed ID: 22172676


  • Jin Y
  • Sultana A
  • Gandhi P
  • Franklin E
  • Hamamoto S
  • Khan AR
  • Munson M
  • Schekman R
  • Weisman LS


Developmental cell

Publication Data

December 13, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM062261
  • Agency: NIGMS NIH HHS, Id: R01 GM062261-09
  • Agency: NIGMS NIH HHS, Id: R01 GM068803
  • Agency: NIGMS NIH HHS, Id: R01 GM068803
  • Agency: NIGMS NIH HHS, Id: R01 GM068803-08
  • Agency: NIGMS NIH HHS, Id: R37 GM062261
  • Agency: NIGMS NIH HHS, Id: R37 GM62261
  • Agency: Howard Hughes Medical Institute, Id:

Mesh Terms

  • Amino Acid Substitution
  • Binding Sites
  • Exocytosis
  • Membrane Fusion
  • Models, Molecular
  • Molecular Motor Proteins
  • Mutagenesis, Site-Directed
  • Myosin Heavy Chains
  • Myosin Type V
  • Protein Interaction Domains and Motifs
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Secretory Vesicles
  • Signal Transduction
  • Vesicular Transport Proteins
  • rab GTP-Binding Proteins