Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation

Chang, Jaerak; Lee, Seongju; Blackstone, Craig

doi:10.1073/pnas.1307391110

Cited by 62 publications

(75 citation statements)

References 44 publications

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“…Moreover, overexpression of the RTN1A isoform caused ER stress in isolated kidney cells, and knockdown of RTN1A attenuates ER stress and renal fibrosis in mice (Fan et al, 2015). In addition, a subset of human hereditary spastic paraplegias is caused by mutations in RTN-2 and Atlastin-1, which also regulates ER morphology (Goyal and Blackstone, 2013; Hu et al, 2009; Chang et al, 2013). Interestingly, Reticulon-4a regulates the ER chaperone protein disulfide isomerase and protects against neurodegeneration in a mouse model of amyotrophic lateral sclerosis (Yang and Strittmatter, 2007).…”

Section: Discussionmentioning

confidence: 99%

Reticulons Regulate the ER Inheritance Block during ER Stress

et al. 2016

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Segregation of functional organelles during the cell cycle is crucial to generate healthy daughter cells. In S. cerevisiae, ER stress causes an ER inheritance block to ensure cells inherit a functional ER. Here, we report that formation of tubular ER in the mother cell, the first step in ER inheritance, depends on functional symmetry between the cortical ER (cER) and perinuclear ER (pnER). ER stress induces functional asymmetry, blocking tubular ER formation and ER inheritance. Using fluorescence recovery after photobleaching, we show that the ER chaperone Kar2/BiP fused to GFP and an ER membrane reporter, Hmg1-GFP, behave differently in the cER and pnER. The functional asymmetry and tubular ER formation depend on Reticulons/Yop1, which maintain ER structure. Lunapark1 deletion in rtn1Δrtn2Δyop1Δ cells restores the pnER/cER functional asymmetry, tubular ER generation and ER inheritance blocks. Thus, Reticulon/Yop1-dependent changes in ER structure are linked to ER inheritance during the yeast cell cycle.

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Section: Discussionmentioning

confidence: 99%

Reticulons Regulate the ER Inheritance Block during ER Stress

et al. 2016

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“…During preparation of the present manuscript, Chang et al (36) described the interaction of protrudin with other HSPrelated proteins in HEK293 cells (a human embryonic kidney cancer cell line) and a role for protrudin in the regulation of ER morphology. Although the results of the two independent studies overlap in part, we adopted a more physiological and comprehensive approach by applying proteomics analysis to neuron-specific protrudin transgenic mice.…”

Section: Discussionmentioning

confidence: 99%

Protrudin Regulates Endoplasmic Reticulum Morphology and Function Associated with the Pathogenesis of Hereditary Spastic Paraplegia

Hashimoto

Shirane

Matsuzaki

et al. 2014

Journal of Biological Chemistry

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Background: Certain hereditary spastic paraplegia (HSP)-related proteins possess hairpin domains and regulate the morphology of the endoplasmic reticulum (ER) network. Results: Protrudin possesses a hairpin domain and interacts with HSP-related proteins. Conclusion: Protrudin regulates ER morphology and function. Significance: Mutant protrudin produced in certain individuals with HSP is prone to form microaggregates that induce ER stress.

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“…Immunoprecipitation and immunoblotting. Immunoprecipitation and immunoblotting were conducted as described previously (40). Cells Figure 11.…”

Section: Methodsmentioning

confidence: 99%

Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation

Chang¹,

Lee²,

Blackstone³

2014

J. Clin. Invest.

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182

230

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Autophagy allows cells to adapt to changes in their environment by coordinating the degradation and recycling of cellular components and organelles to maintain homeostasis. Lysosomes are organelles critical for terminating autophagy via their fusion with mature autophagosomes to generate autolysosomes that degrade autophagic materials; therefore, maintenance of the lysosomal population is essential for autophagy-dependent cellular clearance. Here, we have demonstrated that the two most common autosomal recessive hereditary spastic paraplegia gene products, the SPG15 protein spastizin and the SPG11 protein spatacsin, are pivotal for autophagic lysosome reformation (ALR), a pathway that generates new lysosomes. Lysosomal targeting of spastizin required an intact FYVE domain, which binds phosphatidylinositol 3-phosphate. Loss of spastizin or spatacsin resulted in depletion of free lysosomes, which are competent to fuse with autophagosomes, and an accumulation of autolysosomes, reflecting a failure in ALR. Moreover, spastizin and spatacsin were essential components for the initiation of lysosomal tubulation. Together, these results link dysfunction of the autophagy/lysosomal biogenesis machinery to neurodegeneration.

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Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation

Cited by 62 publications

References 44 publications

Reticulons Regulate the ER Inheritance Block during ER Stress

Reticulons Regulate the ER Inheritance Block during ER Stress

Protrudin Regulates Endoplasmic Reticulum Morphology and Function Associated with the Pathogenesis of Hereditary Spastic Paraplegia

Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation

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