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)20384-9

Cited by 95 publications

(169 citation statements)

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“…Here, we show that Sey1/Atl3 localizes to LCVs in D. discoideum and macrophages and promotes intracellular replication of L. pneumophila by remodeling the ER connecting with the pathogen vacuole. D. discoideum Sey1 shows GTPase activity and is rendered inactive upon mutation of the conserved P-loop lysine residue, similar to other atlastin family members [35,43,44].…”

Section: Discussionmentioning

confidence: 91%

“…Dictyostelium discoideum Sey1 harbors a conserved lysine residue at position 154 in the predicted nucleotide-binding P-loop of the GTPase domain. Mutation of the P-loop lysine to an alanine residue is expected to yield a catalytically inactive, dominant-negative form that is impaired for GTP binding, as shown for S. cerevisiae Sey1p [35] (Appendix Fig S1). Upon production in D. discoideum, GFP-Sey1 K154A did not colocalize with calnexin or PtdIns(4)P ( Fig EV1).…”

Section: Sey1 Localizes To Lcvs and Modulates Replication Of Legionelmentioning

confidence: 92%

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ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila

et al. 2017

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The pathogenic bacterium replicates in host cells within a distinct ER-associated compartment termed the-containing vacuole (LCV). How the dynamic ER network contributes to pathogen proliferation within the nascent LCV remains elusive. A proteomic analysis of purified LCVs identified the ER tubule-resident large GTPase atlastin3 (Atl3, yeast Sey1p) and the reticulon protein Rtn4 as conserved LCV host components. Here, we report that Sey1/Atl3 and Rtn4 localize to early LCVs and are critical for pathogen vacuole formation. Sey1 overproduction promotes intracellular growth of , whereas a catalytically inactive, dominant-negative GTPase mutant protein, or Atl3 depletion, restricts pathogen replication and impairs LCV maturation. Sey1 is not required for initial recruitment of ER to PtdIns(4)-positive LCVs but for subsequent pathogen vacuole expansion. GTP (but not GDP) catalyzes the Sey1-dependent aggregation of purified, ER-positive LCVs Thus, Sey1/Atl3-dependent ER remodeling contributes to LCV maturation and intracellular replication of.

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Section: Discussionmentioning

confidence: 91%

Section: Sey1 Localizes To Lcvs and Modulates Replication Of Legionelmentioning

confidence: 92%

ER remodeling by the large GTPase atlastin promotes vacuolar growth of Legionella pneumophila

et al. 2017

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“…Our conclusions are further strengthened by the finding that intrinsically disordered proteins, which have large hydrodynamic radii yet lack a defined structure, drove fission with substantially greater potency than smaller, structured proteins. membrane fission | membrane traffic | endocytosis | membrane biophysics M embrane fission is required for diverse cellular functions including cytokinesis (1,2), viral egress (3), mitochondrial division (4,5), generation of the endoplasmic reticulum network (6,7), and membrane traffic (8) among others. Despite the essential nature of membrane fission, the energetic barrier to the fission process is substantial.…”

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confidence: 99%

Membrane fission by protein crowding

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Hayden

Gadok

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

153

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Membrane fission, which facilitates compartmentalization of biological processes into discrete, membrane-bound volumes, is essential for cellular life. Proteins with specific structural features including constricting rings, helical scaffolds, and hydrophobic membrane insertions are thought to be the primary drivers of fission. In contrast, here we report a mechanism of fission that is independent of protein structure-steric pressure among membrane-bound proteins. In particular, random collisions among crowded proteins generate substantial pressure, which if unbalanced on the opposite membrane surface can dramatically increase membrane curvature, leading to fission. Using the endocytic protein epsin1 N-terminal homology domain (ENTH), previously thought to drive fission by hydrophobic insertion, our results show that membrane coverage correlates equally with fission regardless of the hydrophobicity of insertions. Specifically, combining FRET-based measurements of membrane coverage with multiple, independent measurements of membrane vesiculation revealed that fission became spontaneous as steric pressure increased. Further, fission efficiency remained equally potent when helices were replaced by synthetic membrane-binding motifs. These data challenge the view that hydrophobic insertions drive membrane fission, suggesting instead that the role of insertions is to anchor proteins strongly to membrane surfaces, amplifying steric pressure. In line with these conclusions, even green fluorescent protein (GFP) was able to drive fission efficiently when bound to the membrane at high coverage. Our conclusions are further strengthened by the finding that intrinsically disordered proteins, which have large hydrodynamic radii yet lack a defined structure, drove fission with substantially greater potency than smaller, structured proteins.

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“…Identifying the proteins mediating positive cellular interactions between lateral line neurons and hair cells, as well as negative interactions between neighboring afferent neurons with different preferences, will provide a molecular paradigm for the segregation and maintenance of neural circuits responding to distinct sensory stimuli. [4,5]. Additional classes of tubular ER proteins, including some REEPs and the ATPase M1 spastin (which severs microtubules), interact with the cytoskeleton [6,7].…”

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confidence: 99%

“…In this latter case, proteins including synaptic glutamate receptors rapidly diffuse within the continuous network of dendritic ER but are confined by increased ER complexity at branch points of dendrites and near dendritic spines. The spatial range of receptor mobility is rapidly restricted by phosphoinositide-linked metabotropic glutamate receptor signaling, which is linked to intracellular Ca 2+ release via inositol (1,4,5) trisphophate (IP 3 ) receptor channels, through a mechanism involving protein kinase C and the ER sheet protein CLIMP63. The morphological changes in local zones of ER have the effect of compartmentalizing ER export and also correspond to sites of new dendritic branches [18].…”

mentioning

confidence: 99%