A Class of Dynamin-like GTPases Involved in the Generation of the Tubular ER Network

Hu, Junjie; Shibata, Yoko; Zhu, Peng; Voss, Christiane; Rismanchi, Neggy; Prinz, William A.; Rapoport, Tom A.; Xu, Chengpei

doi:10.1016/s9999-9994(09)20435-1

Cited by 71 publications

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“…The factors that regulate homotypic ER membrane fusion must also be ER-specific, this is important because the ER is closely apposed and potentially tethered to nearly every membranebound compartment in the cell. Homotypic ER fusion is regulated by the Atlastin family of dynamin-like GTPases (Rismanchi et al 2008;Hu et al 2009;Orso et al 2009;Anwar et al 2012). Atlastin family members localize to the tubular ER and accumulate in a striking pattern at three-way junctions (Fig.…”

Section: Er Dynamics and Assemblymentioning

confidence: 99%

“…Atlastin family members localize to the tubular ER and accumulate in a striking pattern at three-way junctions (Fig. 3C) (Rismanchi et al 2008;Hu et al 2009;Orso et al 2009;Park et al 2010b;Chen et al 2012). Atlastin and its yeast homolog Sey1 do not localize to the NE or to peripheral ER cisternae, suggesting that these proteins belong to a group of proteins that partition to regions of high membrane curvature (Fig.…”

Section: Er Dynamics and Assemblymentioning

confidence: 99%

“…Atlastin and its yeast homolog Sey1 do not localize to the NE or to peripheral ER cisternae, suggesting that these proteins belong to a group of proteins that partition to regions of high membrane curvature (Fig. 3C) (Rismanchi et al 2008;Hu et al 2009;Orso et al 2009;Park et al 2010b). Depletion of endogenous Homo sapiens atl2 and atl3 by siRNA or overexpression of atlastin mutants in HeLa cells results in the formation of long, unbranched ER tubules, presumably as a result of the loss of three-way junctions (Hu et al 2009).…”

Section: Er Dynamics and Assemblymentioning

confidence: 99%

“…3C) (Rismanchi et al 2008;Hu et al 2009;Orso et al 2009;Park et al 2010b). Depletion of endogenous Homo sapiens atl2 and atl3 by siRNA or overexpression of atlastin mutants in HeLa cells results in the formation of long, unbranched ER tubules, presumably as a result of the loss of three-way junctions (Hu et al 2009). In contrast, overexpression of wild-type atlastin in drosophila motor neurons leads to hyper fusion of ER membranes (Orso et al 2009) and an expansion of ER cisternae in mammalian tissue culture cells (Hu et al 2009).…”

Section: Er Dynamics and Assemblymentioning

confidence: 99%

“…Depletion of endogenous Homo sapiens atl2 and atl3 by siRNA or overexpression of atlastin mutants in HeLa cells results in the formation of long, unbranched ER tubules, presumably as a result of the loss of three-way junctions (Hu et al 2009). In contrast, overexpression of wild-type atlastin in drosophila motor neurons leads to hyper fusion of ER membranes (Orso et al 2009) and an expansion of ER cisternae in mammalian tissue culture cells (Hu et al 2009). Proteoliposomes reconstituted with purified atlastin undergo membrane fusion in a GTPdependent manner, providing evidence that atlastins directly regulate ER fusion (Orso et al 2009).…”

Section: Er Dynamics and Assemblymentioning

confidence: 99%

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Endoplasmic Reticulum Structure and Interconnections with Other Organelles

English

Voeltz

2013

Cold Spring Harbor Perspectives in Biology

294

220

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The endoplasmic reticulum (ER) is a large, continuous membrane-bound organelle comprised of functionally and structurally distinct domains including the nuclear envelope, peripheral tubular ER, peripheral cisternae, and numerous membrane contact sites at the plasma membrane, mitochondria, Golgi, endosomes, and peroxisomes. These domains are required for multiple cellular processes, including synthesis of proteins and lipids, calcium level regulation, and exchange of macromolecules with various organelles at ER-membrane contact sites. The ER maintains its unique overall structure regardless of dynamics or transfer at ER-organelle contacts. In this review, we describe the numerous factors that contribute to the structure of the ER.T he endoplasmic reticulum (ER) is a dynamic organelle responsible for many cellular functions, including the synthesis of proteins and lipids, and regulation of intracellular calcium levels. This review focuses on the distinct and complex morphology of the ER. The structure of the ER is complex because of the numerous distinct domains that exist within one continuous membrane bilayer. These domains are shaped by interactions with the cytoskeleton, by proteins that stabilize membrane shape, and by a homotypic fusion machinery that allows the ER membrane to maintain its continuity and identity. The ER also contains domains that contact the plasma membrane (PM) and other organelles including the Golgi, endosomes, mitochondria, lipid droplets, and peroxisomes. ER contact sites with other organelles and the PM are both abundant and dispersed throughout the cytoplasm, suggesting that they too could influence the overall architecture of the ER. As we will discuss here, ER shape and distribution are regulated by many intrinsic and extrinsic forces. ER STRUCTURE AND FORMATION Domains of the ER Are Stabilized by Membrane-Shaping ProteinsThe endoplasmic reticulum (ER) is a large membrane-bound compartment spread throughout the cytoplasm of eukaryotic cells. It is divided into three major morphologies that include the nuclear envelope (NE), peripheral ER cisternae, and an interconnected tubular network

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Section: Er Dynamics and Assemblymentioning

confidence: 99%

Section: Er Dynamics and Assemblymentioning

confidence: 99%

Section: Er Dynamics and Assemblymentioning

confidence: 99%

Section: Er Dynamics and Assemblymentioning

confidence: 99%

Section: Er Dynamics and Assemblymentioning

confidence: 99%

See 3 more Smart Citations

Endoplasmic Reticulum Structure and Interconnections with Other Organelles

English

Voeltz

2013

Cold Spring Harbor Perspectives in Biology

294

220

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Emerging lysosomal pathways for quality control at the endoplasmic reticulum

2019

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Protein misfolding occurring in the endoplasmic reticulum (ER) might eventually lead to aggregation and cellular distress, and is a primary pathogenic mechanism in multiple human disorders. Mammals have developed evolutionary‐conserved quality control mechanisms at the level of the ER. The best characterized is the ER‐associated degradation (ERAD) pathway, through which misfolded proteins translocate from the ER to the cytosol and are subsequently proteasomally degraded. However, increasing evidence indicates that additional quality control mechanisms apply for misfolded ER clients that are not eligible for ERAD. This review focuses on the alternative, ERAD‐independent, mechanisms of clearance of misfolded polypeptides from the ER. These processes, collectively referred to as ER‐to‐lysosome–associated degradation, involve ER‐phagy, microautophagy or vesicular transport. The identification of the underlying molecular mechanisms is particularly important for developing new therapeutic approaches for human diseases associated with protein aggregate formation.

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The axonal endoplasmic reticulum: One organelle—many functions in development, maintenance, and plasticity

Luarte

Cornejo

Bertin

et al. 2017

Developmental Neurobiology

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The endoplasmic reticulum (ER) is highly conserved in eukaryotes and neurons. Indeed, the localization of the organelle in axons has been known for nearly half a century. However, the relevance of the axonal ER is only beginning to emerge. In this review, we discuss the structure of the ER in axons, examining the role of ER-shaping proteins and highlighting reticulons. We analyze the multiple functions of the ER and their potential contribution to axonal physiology. First, we examine the emerging roles of the axonal ER in lipid synthesis, protein translation, processing, quality control, and secretory trafficking of transmembrane proteins. We also review the impact of the ER on calcium dynamics, focusing on intracellular mechanisms and functions. We describe the interactions between the ER and endosomes, mitochondria, and synaptic vesicles. Finally, we analyze available proteomic data of axonal preparations to reveal the dynamic functionality of the ER in axons during development. We suggest that the dynamic proteome and a validated axonal interactome, together with state-of-the-art methodologies, may provide interesting research avenues in axon physiology that may extend to pathology and regeneration. © 2017 Wiley Periodicals, Inc. Develop Neurobiol 78: 181-208, 2018.

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A Class of Dynamin-like GTPases Involved in the Generation of the Tubular ER Network

Cited by 71 publications

References 0 publications

Endoplasmic Reticulum Structure and Interconnections with Other Organelles

Endoplasmic Reticulum Structure and Interconnections with Other Organelles

Emerging lysosomal pathways for quality control at the endoplasmic reticulum

The axonal endoplasmic reticulum: One organelle—many functions in development, maintenance, and plasticity

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