Talk:2010 Lecture 3

From CellBiology

JCB Movies

  • A myosin V moves yeast secretory vesicles Secretory vesicles actively move to the site of exocytosis in yeast. Schott et al. find that multiple secretory vesicles often follow the same linear track and frequently enter and cross the bud. This movement requires the activity of the myosin-V heavy chain encoded by the MYO2 gene. When the predicted lever arm of this motor is progressively shortened (with the most extreme example being the 0IQ mutant), the vesicle movements are progressively slowed.
  • Rapid cycling of lipid rafts to and from the Golgi Nichols et al. detect rapid cycling of lipid raft markers between the plasma membrane and the Golgi. Through selective photobleaching, they are able to study transport either out from the Golgi to the plasma membrane, or in from the plasma membrane to the Golgi.
  • Membrane docking at the immunological synapse requires Rab27a Stinchcombe et al. find that normal membrane docking of lytic granules at the immunological synapse is defective in cells lacking Rab27a. In cells lacking other Rab proteins, polarization of the secretory granules is incomplete.
  • Visualizing the location and dynamics of exocytosis Schmoranzer et al. use total internal reflection (TIR) fluorescence microscopy to visualize exocytosis in mammalian cells (e.g., see event on left side of video). The analysis reveals that there are no preferred sites for constitutive exocytosis in this system.
  • Visualizing the location and dynamics of exocytosis Toomre et al. use a combination of TIR microscopy (green, labeling molecules close to or at the membrane) and standard fluorescence microscopy (red, for molecules further from the membrane) to visualize [/content/vol149/issue1/images/data/33/DC1/ trafficking to and fusion with] the plasma membrane during exocytosis. Red dots turn yellow then green as they approach the membrane, and then explode in a burst of light as they fuse with the plasma membrane during exocytosis. The transport containers appear to be partially anchored at the membrane before fusion, and can undergo either partial or complete fusion events.

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PLoS Movies

Working Area

The following material is a draft notebook area, not part of the current lecture content.

  • Vertebrate membrane proteins: structure, function, and insights from biophysical approaches. Müller DJ, Wu N, Palczewski K. Pharmacol Rev. 2008 Mar;60(1):43-78. Epub 2008 Mar 5. Review. PMID: 18321962
  • Cell motility through plasma membrane blebbing Oliver T. Fackler and Robert Grosse J Cell Biol. 2008 June 16; 181(6): 879–884. doi: 10.1083/jcb.200802081. PMCID: PMC2426937
  • Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. Morone N, Fujiwara T, Murase K, Kasai RS, Ike H, Yuasa S, Usukura J, Kusumi A. J Cell Biol. 2006 Sep 11;174(6):851-62. Epub 2006 Sep 5. PMID: 1695434 JCB