title: GRASPing unconventional secretion.
abstract: GRASP proteins associate with the Golgi apparatus and have been implicated in the stacking of Golgi cisternae, vesicle tethering, and mitotic progression, but their specific functions are unclear. In this issue, Kinseth et al. (2007) show unexpectedly that a GRASP homolog is required for an unconventional secretory pathway that bypasses the usual route for Golgi-dependent membrane traffic.
authors: Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA.
authors: Stephanie K
authors: SK
authors: Levi
authors: Benjamin S
authors: BS
authors: Glick
mesh_terms: D000818:Animals; D004023:Dictyostelium / Q000737:chemistry / Q000502:physiology; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism*; D006056:Golgi Apparatus / Q000737:chemistry / Q000502:physiology*; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D029721:Drosophila Proteins; C506558:GRASP65 protein, Drosophila; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins