The Experts below are selected from a list of 225 Experts worldwide ranked by ideXlab platform
Daniel J Klionsky - One of the best experts on this subject based on the ideXlab platform.
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a novel Reticulophagy receptor epr1 a bridge between the phagophore protein atg8 and er transmembrane vap proteins
Autophagy, 2020Co-Authors: Ying Yang, Daniel J KlionskyAbstract:Reticulophagy, a type of selective autophagy that specifically targets and degrades parts of the endoplasmic reticulum (ER) network (sheets or tubules), plays a crucial role in the responses to ER stress. The selectivity of the ER cargo recognition relies on the unique Reticulophagy receptors, which tether and deliver cargos to phagophores, the precursors to autophagosomes. Various integral membrane proteins have been well characterized as Reticulophagy receptors, including Atg39, Atg40, RETREG1/FAM134B, SEC62, RTN3L, CCPG1, TEX264, and ATL3, in both yeast and mammals in the past five years. In a recent paper, Zhao et al. discovered in fission yeast a novel Reticulophagy receptor, Epr1, which bridges the ER and phagophore by binding to Atg8 and VAPs, a mechanism different from the aforementioned Reticulophagy receptors.
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molecular dynamics simulations reveal how the reticulon homology domain of the autophagy receptor retreg1 fam134b remodels membranes for efficient selective Reticulophagy
Autophagy, 2020Co-Authors: Hana Popelka, Daniel J KlionskyAbstract:ABSTRACTThe autophagy receptor for selective Reticulophagy, RETREG1/FAM134B is essential for ER maintenance, and its dysfunction is associated with neuronal disorders, vascular dementia, or viral i...
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Molecular dynamics simulations reveal how the reticulon-homology domain of the autophagy receptor RETREG1/FAM134B remodels membranes for efficient selective Reticulophagy.
Autophagy, 2020Co-Authors: Hana Popelka, Daniel J KlionskyAbstract:The autophagy receptor for selective Reticulophagy, RETREG1/FAM134B is essential for ER maintenance, and its dysfunction is associated with neuronal disorders, vascular dementia, or viral infections. The protein consists of the reticulon-homology domain (RHD) that is flanked at the N- and C-termini by an intrinsically disordered protein region (IDPR), where the C terminal IDPR carries the indispensable LC3-interacting region (LIR) motif for the interaction with LC3. The RHD of RETREG1 is presumed to play a role in membrane remodeling, but the absence of a known 3D structure of this domain so far prevented researchers from gaining mechanistic insights into how the RETREG1 RHD curves membranes, and thereby facilities Reticulophagy. The recent study by Bhaskara et al., which is described in this editor's corner article, used molecular dynamics (MD) simulations to create a structural model of the RETREG1 RHD. MD simulations along with in vitro liposome remodeling experiments reveal how the RHD domain acts on the ER membrane and, in concert with the C terminal IDPR, executes the function of RETREG1 in selective Reticulophagy.Abbreviations: ER, endoplasmic reticulum; IDPR, intrinsically disordered protein region; LIR, LC3-interacting region; MD, molecular dynamics; RHD, reticulon-homology domain; TM, transmembrane.
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molecular dynamics simulations reveal how the reticulon homology domain of the autophagy receptor retreg1 fam134b remodels membranes for efficient selective Reticulophagy
Autophagy, 2020Co-Authors: Hana Popelka, Daniel J KlionskyAbstract:The autophagy receptor for selective Reticulophagy, RETREG1/FAM134B is essential for ER maintenance, and its dysfunction is associated with neuronal disorders, vascular dementia, or viral infections. The protein consists of the reticulon-homology domain (RHD) that is flanked at the N- and C-termini by an intrinsically disordered protein region (IDPR), where the C terminal IDPR carries the indispensable LC3-interacting region (LIR) motif for the interaction with LC3. The RHD of RETREG1 is presumed to play a role in membrane remodeling, but the absence of a known 3D structure of this domain so far prevented researchers from gaining mechanistic insights into how the RETREG1 RHD curves membranes, and thereby facilities Reticulophagy. The recent study by Bhaskara et al., which is described in this editor's corner article, used molecular dynamics (MD) simulations to create a structural model of the RETREG1 RHD. MD simulations along with in vitro liposome remodeling experiments reveal how the RHD domain acts on the ER membrane and, in concert with the C terminal IDPR, executes the function of RETREG1 in selective Reticulophagy.Abbreviations: ER, endoplasmic reticulum; IDPR, intrinsically disordered protein region; LIR, LC3-interacting region; MD, molecular dynamics; RHD, reticulon-homology domain; TM, transmembrane.
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TEX264 is a major receptor for mammalian Reticulophagy.
Autophagy, 2019Co-Authors: Elizabeth Delorme-axford, Hana Popelka, Daniel J KlionskyAbstract:ABSTRACTThe endoplasmic reticulum (ER) is the main site of cellular protein and calcium homeostasis, as well as lipid synthesis in eukaryotic cells. Reticulophagy is the selective clearance and deg...
Thierry Galli - One of the best experts on this subject based on the ideXlab platform.
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introducing secretory Reticulophagy er phagy serp a vamp7 dependent pathway involved in neurite growth
Autophagy, 2021Co-Authors: Somya Vats, Thierry GalliAbstract:Together with the proteasome, macroautophagy is a main pathway for the degradation of intracellular elements. Endoplasmic reticulum (ER)-autophagy i.e. Reticulophagy/ER-phagy leads to the encapsulation of pieces of the ER in forming autophagosomes. This is generally followed by fusion with lysosomes and degradation of these ER components by lysosomal hydrolases. Recent work by our group shows that ER elements could also be incorporated into late endosomes and later be released by a secretory mechanism which we will herein refer to as secretory Reticulophagy/ER-phagy (SERP). In the absence of macroautophagy, such as by knocking out Atg5, SERP is more efficient, leading to an increased secretion of MAP1LC3B-II and LC3-interacting region (LIR)-containing proteins of the ER, reticulons and atlastins. In this scenario, neurites grow longer and neuronal polarity is altered. In the absence of SERP, such as by knocking out Vamp7, secretion of MAP1LC3B-II, ER-LIR containing proteins and neurite growth are severely inhibited. We argue that SERP might be a main secretory mechanism bypassing the Golgi apparatus, and that it is particularly active and important in neurite growth.
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Introducing secretory Reticulophagy/ER-phagy (SERP), a VAMP7-dependent pathway involved in neurite growth
Autophagy, 2021Co-Authors: Somya Vats, Thierry GalliAbstract:Together with the proteasome, macroautophagy is a main pathway for the degradation of intracellular elements. Endoplasmic reticulum (ER)-autophagy i.e. Reticulophagy/ERphagy leads to the encapsulation of pieces of the ER in forming autophagosomes. This is generally followed by fusion with lysosomes and degradation of these ER components by lysosomal hydrolases. Recent work by our group shows that ER elements could also be incorporated into late endosomes and later be released by a secretory mechanism which we will herein refer to as secretory Reticulophagy/ERphagy (SERP). In the absence of macroautophagy, such as by knocking out Atg5, SERP is more efficient, leading to an increased secretion of MAP1LC3B-II and LC3interacting region (LIR)-containing proteins of the ER, reticulons and atlastins. In this scenario, neurites grow longer and neuronal polarity is altered. In the absence of SERP, such as by knocking out Vamp7, secretion of MAP1LC3B-II, ER-LIR containing proteins and neurite growth are severely inhibited. We argue that SERP might be a main secretory mechanism bypassing the Golgi apparatus, and that it is particularly active and important in neurite growth.
Somya Vats - One of the best experts on this subject based on the ideXlab platform.
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introducing secretory Reticulophagy er phagy serp a vamp7 dependent pathway involved in neurite growth
Autophagy, 2021Co-Authors: Somya Vats, Thierry GalliAbstract:Together with the proteasome, macroautophagy is a main pathway for the degradation of intracellular elements. Endoplasmic reticulum (ER)-autophagy i.e. Reticulophagy/ER-phagy leads to the encapsulation of pieces of the ER in forming autophagosomes. This is generally followed by fusion with lysosomes and degradation of these ER components by lysosomal hydrolases. Recent work by our group shows that ER elements could also be incorporated into late endosomes and later be released by a secretory mechanism which we will herein refer to as secretory Reticulophagy/ER-phagy (SERP). In the absence of macroautophagy, such as by knocking out Atg5, SERP is more efficient, leading to an increased secretion of MAP1LC3B-II and LC3-interacting region (LIR)-containing proteins of the ER, reticulons and atlastins. In this scenario, neurites grow longer and neuronal polarity is altered. In the absence of SERP, such as by knocking out Vamp7, secretion of MAP1LC3B-II, ER-LIR containing proteins and neurite growth are severely inhibited. We argue that SERP might be a main secretory mechanism bypassing the Golgi apparatus, and that it is particularly active and important in neurite growth.
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Introducing secretory Reticulophagy/ER-phagy (SERP), a VAMP7-dependent pathway involved in neurite growth
Autophagy, 2021Co-Authors: Somya Vats, Thierry GalliAbstract:Together with the proteasome, macroautophagy is a main pathway for the degradation of intracellular elements. Endoplasmic reticulum (ER)-autophagy i.e. Reticulophagy/ERphagy leads to the encapsulation of pieces of the ER in forming autophagosomes. This is generally followed by fusion with lysosomes and degradation of these ER components by lysosomal hydrolases. Recent work by our group shows that ER elements could also be incorporated into late endosomes and later be released by a secretory mechanism which we will herein refer to as secretory Reticulophagy/ERphagy (SERP). In the absence of macroautophagy, such as by knocking out Atg5, SERP is more efficient, leading to an increased secretion of MAP1LC3B-II and LC3interacting region (LIR)-containing proteins of the ER, reticulons and atlastins. In this scenario, neurites grow longer and neuronal polarity is altered. In the absence of SERP, such as by knocking out Vamp7, secretion of MAP1LC3B-II, ER-LIR containing proteins and neurite growth are severely inhibited. We argue that SERP might be a main secretory mechanism bypassing the Golgi apparatus, and that it is particularly active and important in neurite growth.
Hana Popelka - One of the best experts on this subject based on the ideXlab platform.
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molecular dynamics simulations reveal how the reticulon homology domain of the autophagy receptor retreg1 fam134b remodels membranes for efficient selective Reticulophagy
Autophagy, 2020Co-Authors: Hana Popelka, Daniel J KlionskyAbstract:ABSTRACTThe autophagy receptor for selective Reticulophagy, RETREG1/FAM134B is essential for ER maintenance, and its dysfunction is associated with neuronal disorders, vascular dementia, or viral i...
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Molecular dynamics simulations reveal how the reticulon-homology domain of the autophagy receptor RETREG1/FAM134B remodels membranes for efficient selective Reticulophagy.
Autophagy, 2020Co-Authors: Hana Popelka, Daniel J KlionskyAbstract:The autophagy receptor for selective Reticulophagy, RETREG1/FAM134B is essential for ER maintenance, and its dysfunction is associated with neuronal disorders, vascular dementia, or viral infections. The protein consists of the reticulon-homology domain (RHD) that is flanked at the N- and C-termini by an intrinsically disordered protein region (IDPR), where the C terminal IDPR carries the indispensable LC3-interacting region (LIR) motif for the interaction with LC3. The RHD of RETREG1 is presumed to play a role in membrane remodeling, but the absence of a known 3D structure of this domain so far prevented researchers from gaining mechanistic insights into how the RETREG1 RHD curves membranes, and thereby facilities Reticulophagy. The recent study by Bhaskara et al., which is described in this editor's corner article, used molecular dynamics (MD) simulations to create a structural model of the RETREG1 RHD. MD simulations along with in vitro liposome remodeling experiments reveal how the RHD domain acts on the ER membrane and, in concert with the C terminal IDPR, executes the function of RETREG1 in selective Reticulophagy.Abbreviations: ER, endoplasmic reticulum; IDPR, intrinsically disordered protein region; LIR, LC3-interacting region; MD, molecular dynamics; RHD, reticulon-homology domain; TM, transmembrane.
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molecular dynamics simulations reveal how the reticulon homology domain of the autophagy receptor retreg1 fam134b remodels membranes for efficient selective Reticulophagy
Autophagy, 2020Co-Authors: Hana Popelka, Daniel J KlionskyAbstract:The autophagy receptor for selective Reticulophagy, RETREG1/FAM134B is essential for ER maintenance, and its dysfunction is associated with neuronal disorders, vascular dementia, or viral infections. The protein consists of the reticulon-homology domain (RHD) that is flanked at the N- and C-termini by an intrinsically disordered protein region (IDPR), where the C terminal IDPR carries the indispensable LC3-interacting region (LIR) motif for the interaction with LC3. The RHD of RETREG1 is presumed to play a role in membrane remodeling, but the absence of a known 3D structure of this domain so far prevented researchers from gaining mechanistic insights into how the RETREG1 RHD curves membranes, and thereby facilities Reticulophagy. The recent study by Bhaskara et al., which is described in this editor's corner article, used molecular dynamics (MD) simulations to create a structural model of the RETREG1 RHD. MD simulations along with in vitro liposome remodeling experiments reveal how the RHD domain acts on the ER membrane and, in concert with the C terminal IDPR, executes the function of RETREG1 in selective Reticulophagy.Abbreviations: ER, endoplasmic reticulum; IDPR, intrinsically disordered protein region; LIR, LC3-interacting region; MD, molecular dynamics; RHD, reticulon-homology domain; TM, transmembrane.
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TEX264 is a major receptor for mammalian Reticulophagy.
Autophagy, 2019Co-Authors: Elizabeth Delorme-axford, Hana Popelka, Daniel J KlionskyAbstract:ABSTRACTThe endoplasmic reticulum (ER) is the main site of cellular protein and calcium homeostasis, as well as lipid synthesis in eukaryotic cells. Reticulophagy is the selective clearance and deg...
Hitoshi Nakatogawa - One of the best experts on this subject based on the ideXlab platform.
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Atg8-mediated super-assembly of Atg40 induces local ER remodeling in Reticulophagy.
Autophagy, 2020Co-Authors: Keisuke Mochida, Hitoshi NakatogawaAbstract:Reticulophagy (or ER-phagy) is a type of selective autophagy that targets the endoplasmic reticulum (ER). In the process of Reticulophagy, part of the ER is fragmented and packed within autophagoso...
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Reticulophagy and nucleophagy: New findings and unsolved issues.
Autophagy, 2015Co-Authors: Hitoshi Nakatogawa, Keisuke MochidaAbstract:Autophagy targets various intracellular components ranging from proteins and nucleic acids to organelles for their degradation in lysosomes or vacuoles. In selective types of autophagy, receptor proteins play central roles in target selection. These proteins bind or localize to specific targets, and also interact with Atg8 family proteins on forming autophagosomal membranes, leading to the efficient sequestration of the targets by the membranes. Our recent study revealed that yeast cells actively degrade the endoplasmic reticulum (ER) and even part of the nucleus via selective autophagy under nitrogen-deprived conditions. We identified novel receptors, Atg39 and Atg40, specific to these pathways. Here, we summarize our findings on 'Reticulophagy' (or 'ER-phagy') and 'nucleophagy', and discuss key issues that remain to be solved in future studies.