PMID: 9164844May 15, 1997Paper

Characterization of Rab3A, Rab3B and Rab3C: different biochemical properties and intracellular localization in bovine chromaffin cells

The Biochemical Journal
C G LinL S Kao

Abstract

In this study we examined the biochemical properties and subcellular localization of Rab3A, Rab3B and Rab3C in bovine adrenal chromaffin cells. The Kd for guanosine 5'-[gamma-thio]triphosphate (GTP[S]) of the three Rab3 proteins was 15, 2700 and 204 nM for Rab3A, Rab3B and Rab3C respectively. The intrinsic GTPase activity of the three Rab3 proteins seemed similar and was increased approx. 3-fold by bovine chromaffin cell lysate. Truncation of the C-terminal 31 amino acid residues decreased the binding affinity for GTP[S] of the three Rab3 proteins. When the C-terminus of Rab3C was replaced with that of Rab3A, the binding affinity of Rab3C for GTP[S] was decreased, but the replacement did not affect the affinity of Rab3B for GTP[S]. Immunostaining experiments showed that Rab3A, Rab3B and Rab3C are localized separately within chromaffin cells. Anti-Rab3A and anti-Rab3C antibodies stained vesicle-like structures, whereas anti-Rab3B antibody distinctly stained the plasma membrane. In summary, bovine chromaffin cells express the three Rab3 proteins but the subcellular localization and biochemical properties of the three Rab3 proteins are distinct.

Citations

Jun 15, 2000·Experimental Cell Research·C SunshineK L Kirk
Jul 5, 2006·Cell and Tissue Research·Ute Becherer, Jens Rettig
Jul 11, 2006·American Journal of Physiology. Cell Physiology·M RupnikR Zorec
Aug 9, 2002·The Journal of Biological Chemistry·Oliver M SchlüterThomas C Südhof
Dec 14, 2001·Biochemical and Biophysical Research Communications·R S Sidhu, R P Bhullar
Mar 2, 1999·Biochemical and Biophysical Research Communications·Z HuangE Slatopolsky

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