QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Steegmaier, M. Articles by Scheller, R. H. Search for Related Content PubMed PubMed Citation Articles by Steegmaier, M. Articles by Scheller, R. H.

Vol. 11, Issue 8, 2719-2731, August 2000

Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

Martin Steegmaier,^* Viola Oorschot, Judith Klumperman, and Richard H. Scheller^*

 ^*Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305-5345; and  Department of Cell Biology, School of Medicine, Research Institute for Biomembranes, University of Utrecht, 3584CX Utrecht, The Netherlands

The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular ER membranes that are abundant in steroidogenic cells.

---

Corresponding author. E-mail address: scheller{at}cmgm.stanford.edu.

---

Molecular Biology of the Cell
Vol. 11, 2719-2731, August 2000
Copyright © 2000 by The American Society for Cell Biology

This article has been cited by other articles:

				T. H. Kloepper, C. N. Kienle, and D. Fasshauer SNAREing the Basis of Multicellularity: Consequences of Protein Family Expansion during Evolution Mol. Biol. Evol., September 1, 2008; 25(9): 2055 - 2068. [Abstract] [Full Text] [PDF]

				Q. Zhang, J. Li, M. Deavers, J. L. Abbruzzese, and L. Ho The Subcellular Localization of Syntaxin 17 Varies Among Different Cell Types and Is Altered in Some Malignant Cells J. Histochem. Cytochem., November 1, 2005; 53(11): 1371 - 1382. [Abstract] [Full Text] [PDF]

				E.-M. Damm, L. Pelkmans, J. Kartenbeck, A. Mezzacasa, T. Kurzchalia, and A. Helenius Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae J. Cell Biol., January 31, 2005; 168(3): 477 - 488. [Abstract] [Full Text] [PDF]

				H. Hasegawa, Z. Yang, L. Oltedal, S. Davanger, and J. C. Hay Intramolecular protein-protein and protein-lipid interactions control the conformation and subcellular targeting of neuronal Ykt6 J. Cell Sci., September 1, 2004; 117(19): 4495 - 4508. [Abstract] [Full Text] [PDF]

				H. Hasegawa, S. Zinsser, Y. Rhee, E. O. Vik-Mo, S. Davanger, and J. C. Hay Mammalian Ykt6 Is a Neuronal SNARE Targeted to a Specialized Compartment by its Profilin-like Amino Terminal Domain Mol. Biol. Cell, February 1, 2003; 14(2): 698 - 720. [Abstract] [Full Text] [PDF]

				A. A. Peden, G. Y. Park, and R. H. Scheller The Di-leucine Motif of Vesicle-associated Membrane Protein 4 Is Required for Its Localization and AP-1 Binding J. Biol. Chem., December 21, 2001; 276(52): 49183 - 49187. [Abstract] [Full Text] [PDF]