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Rab4
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Abstract
Rab4 was first localized to early endosomes by screening subcellular fractions prepared from CHO cells using the original panel of polyclonal anti-rab antibodies prepared by Bruno Goud3 Free-flow electrophoresis fractions were analyzed by immunoblotting, and only antibody to rab4 was found to yield a clear signal in the anodally-shifted fractions that co-migrated with transferrin receptor. This localization was confirmed by immunofluorescence performed on cells (Hela, CHO) stably or transiently transfected with wild type rab4a cDNAs. lmmunoelectron microscopy (immuno-EM) on frozen thin sections is also consistent with an early endosome/recycling vesicle localization4; very little rab4 is detectable on the plasma membrane. Since rab5 has also been localized by immunofluorescence, cell fractionation, and immune-EM to early endocytic compartments (see rab5 entry, p. 295), it has been presumed that rab4 and rab5 are themselves co-localized.
Title: Rab4
Description:
Abstract
Rab4 was first localized to early endosomes by screening subcellular fractions prepared from CHO cells using the original panel of polyclonal anti-rab antibodies prepared by Bruno Goud3 Free-flow electrophoresis fractions were analyzed by immunoblotting, and only antibody to rab4 was found to yield a clear signal in the anodally-shifted fractions that co-migrated with transferrin receptor.
This localization was confirmed by immunofluorescence performed on cells (Hela, CHO) stably or transiently transfected with wild type rab4a cDNAs.
lmmunoelectron microscopy (immuno-EM) on frozen thin sections is also consistent with an early endosome/recycling vesicle localization4; very little rab4 is detectable on the plasma membrane.
Since rab5 has also been localized by immunofluorescence, cell fractionation, and immune-EM to early endocytic compartments (see rab5 entry, p.
295), it has been presumed that rab4 and rab5 are themselves co-localized.
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