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Department of Biochemistry and Molecular Biology and Center for
Basic Research in Digestive Diseases, Mayo Clinic and Foundation,
Rochester, Minnesota 55905
Dynamins are 100-kDa GTPases that are essential for clathrin-coated
vesicle formation during receptor-mediated endocytosis. To date, three
different dynamin genes have been identified, with each gene expressing
at least four different alternatively spliced forms. Currently, it is
unclear whether these different dynamin gene products perform distinct
or redundant cellular functions. Therefore, the focus of this study was
to identify additional spliced variants of dynamin from rat tissues and
to define the distribution of the dynamin family members in a cultured
rat epithelial cell model (Clone 9 cells). After long-distance reverse
transcription (RT)-PCR of mRNA from different rat tissues, the
full-length cDNAs encoding the different dynamin isoforms were
sequenced and revealed four additional spliced variants for dynamin
I and nine for dynamin III. Thus, in rat tissues there are a
total of at least 25 different mRNAs produced from the three dynamin
genes. Subsequently, we generated stably transfected Clone 9 cells
expressing full-length cDNAs of six different spliced forms tagged with
green fluorescent protein. Confocal or fluorescence microscopy of these
transfected cells revealed that many of the dynamin proteins associate
with distinct membrane compartments, which include clathrin-coated pits
at the plasma membrane and the Golgi apparatus, and several undefined
vesicle populations. These results indicate that the dynamin family is
more extensive than was originally predicted and suggest that the
different dynamin proteins are localized to distinct cytoplasmic or
membrane compartments.
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