The role of ankyrin and spectrin in membrane transport and domain formation.
Recent discoveries reveal a Golgi-centric spectrin-ankyrin skeleton required for Golgi integrity and anterograde protein trafficking. Identification of specific functional domains in spectrin that mediate its association with motor proteins and the Golgi complex has allowed novel insights into the structure and function of the secretory pathway, and into how this process is controlled by ADP-ribosylation factor and phosphoinositides. Alternative models of Golgi spectrin function that have been recently proposed are reviewed.
De Matteis
M A
MA
Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Santa Maria Imbaro, Chieti, Italy. dematte@cmns.mnegri.it
Morrow
J S
JS
D020727:ADP-Ribosylation Factors; D017487:Ankyrins / Q000378:metabolism*; D001692:Biological Transport; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000502:physiology; D006056:Golgi Apparatus / Q000378:metabolism; D010716:Phosphatidylinositols / Q000502:physiology; D013049:Spectrin / Q000378:metabolism*
D017487:Ankyrins; D010716:Phosphatidylinositols; D013049:Spectrin; D019204:GTP-Binding Proteins; D020727:ADP-Ribosylation Factors