Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 18 September 2001
Vol. 2001, Issue 100, p. re11
[DOI: 10.1126/stke.2001.100.re11]


Ypt/Rab GTPases: Regulators of Protein Trafficking

Nava Segev

The author is in the Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, MBRB 4120, 900 South Ashland Avenue, Chicago, IL 60607, USA. E-mail: nava{at}

Abstract: Ypt/Rab guanosine triphosphatases (GTPases) have emerged in the last decade as key regulators of protein transport in all eukaryotic cells. They seem to be involved in all aspects of vesicle trafficking: vesicle formation, motility, and docking, and membrane remodeling and fusion. The functions of Ypt/Rabs are themselves controlled by upstream regulators that stimulate both their nucleotide cycling and their cycling between membranes. Ypt/Rabs transmit signals to downstream effectors in a guanosine triphosphate (GTP)-dependent manner. The identity of upstream regulators and downstream effectors is known for a number of Ypt/Rabs, and models for their mechanisms of action are emerging. In at least two cases, Ypt/Rab upstream regulators and downstream effectors are found together in a single complex. In agreement with the idea that Ypt/Rabs function in all aspects of vesicular transport, their diverse effectors have recently been shown to function in all identified aspects of vesicle transport. Activators and effectors for individual Ypt/Rabs share no similarity, but are conserved between yeast and mammalian cells. Finally, cross talk demonstrated among the various Ypt/Rabs, and between Ypt/Rabs and other signaling factors, suggests possible coordination among secretory steps, as well as between protein transport and other cellular processes.

Citation: N. Segev, Ypt/Rab GTPases: Regulators of Protein Trafficking. Sci. STKE 2001, re11 (2001).

Read the Full Text

Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi.
M. J. Kwon, M. Arentshorst, M. Fiedler, F. L. M. de Groen, P. J. Punt, V. Meyer, and A. F. J. Ram (2014)
Microbiology 160, 316-329
   Abstract »    Full Text »    PDF »
Rab11-family interacting proteins define spatially and temporally distinct regions within the dynamic Rab11a-dependent recycling system.
N. W. Baetz and J. R. Goldenring (2013)
Mol. Biol. Cell 24, 643-658
   Abstract »    Full Text »    PDF »
Optineurin mediates a negative regulation of Rab8 by the GTPase-activating protein TBC1D17.
V. Vaibhava, A. Nagabhushana, M. L. S. Chalasani, C. Sudhakar, A. Kumari, and G. Swarup (2012)
J. Cell Sci. 125, 5026-5039
   Abstract »    Full Text »    PDF »
Dynamic of Ion Channel Expression at the Plasma Membrane of Cardiomyocytes.
E. Balse, D. F. Steele, H. Abriel, A. Coulombe, D. Fedida, and S. N. Hatem (2012)
Physiol Rev 92, 1317-1358
   Abstract »    Full Text »    PDF »
Modular TRAPP Complexes Regulate Intracellular Protein Trafficking Through Multiple Ypt/Rab GTPases in Saccharomyces cerevisiae.
S. Zou, Y. Liu, X. Q. Zhang, Y. Chen, M. Ye, X. Zhu, S. Yang, Z. Lipatova, Y. Liang, and N. Segev (2012)
Genetics 191, 451-460
   Abstract »    Full Text »    PDF »
Regulation of selective autophagy onset by a Ypt/Rab GTPase module.
Z. Lipatova, N. Belogortseva, X. Q. Zhang, J. Kim, D. Taussig, and N. Segev (2012)
PNAS 109, 6981-6986
   Abstract »    Full Text »    PDF »
Rab11b regulates the trafficking and recycling of the epithelial sodium channel (ENaC).
M. B. Butterworth, R. S. Edinger, M. R. Silvis, L. I. Gallo, X. Liang, G. Apodaca, R. A. Fizzell, and J. P. Johnson (2012)
Am J Physiol Renal Physiol 302, F581-F590
   Abstract »    Full Text »    PDF »
Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase Ypt52 and inhibits Ypt52 function.
Y. Liu, K. Nakatsukasa, M. Kotera, A. Kanada, T. Nishimura, T. Kishi, S. Mimura, and T. Kamura (2011)
Mol. Biol. Cell 22, 1575-1584
   Abstract »    Full Text »    PDF »
A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1.
X. Hou, N. Hagemann, S. Schoebel, W. Blankenfeldt, R. S. Goody, K. S. Erdmann, and A. Itzen (2011)
EMBO J. 30, 1659-1670
   Abstract »    Full Text »    PDF »
The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p.
B. L. Grosshans, A. Andreeva, A. Gangar, S. Niessen, J. R. Yates III, P. Brennwald, and P. Novick (2006)
J. Cell Biol. 172, 55-66
   Abstract »    Full Text »    PDF »
Human RAS Superfamily Proteins and Related GTPases.
J. Colicelli (2004)
Sci. STKE 2004, re13
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882