A budding and fusing journey through the secretory pathway. Genetic and In Vitro Analysis of Cell Compartmentalization: A UCLA symposium, Taos, NM, USA, February 3-9, 1990.
Reconstitution of vesicular transport events and the molecular and genetic analysis of the secretory pathway have taken the field of membrane traffic into a new era. Already, proteins have been discovered that facilitate multiple transport steps, and studies of the identities and modes of action of additional transport components, such as those that specify the targets of transport vesicles, will soon follow. Even after we understand how transport vesicles form, find their targets, and then fuse, other fundamental questions will still remain. How are proteins sorted into distinct transport vesicles? How is the directionality of protein transport achieved? How do organelles maintain their identities in the face of large volumes of membrane traffic? Finally, how is membrane traffic regulated? Answers to each of these fundamental questions are likely to be available in the not-too-distant future.
Pfeffer
S R
SR
Department of Biochemistry, Stanford University School of Medicine, CA 94305.
D000818:Animals; D001692:Biological Transport; D002451:Cell Compartmentation; D003594:Cytoplasmic Granules / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D009516:New Mexico; D011506:Proteins / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism*
D011506:Proteins; D019204:GTP-Binding Proteins