Abstract
The existence of a Golgi-localized membrane cytoskeleton has been revealed by the identification of two major components of the spectrin membrane skeleton, spectrin and ankyrin, that associate with the Golgi complex. Golgi spectrin was identified with an antibody specific for the β-subunit of the erythroid isoform of spectrin (β1Σ1). This antibody recognizes a 220 kDa polypeptide that localizes to discrete regions of the Golgi complex and associates with Golgi membranes in a Brefeldin A sensitive manner. Two isoforms of Golgi ankyrin have been identified: a 119 kDa form (Ank G119) which represents a truncated, alternatively spliced isoform of a recently cloned novel ankyrin of the nervous system Ank G, and a larger 195 kDa ankyrin (Ank 195) that cross-reacts with antibodies to erythrocyte ankyrin. A Golgi localized membrane skeleton composed of these unique membrane skeleton isoforms could serve a variety of important functions, including the maintenance of Golgi structural organization and the formation of discrete membrane domains within Golgi compartments.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
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