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The Arp2/3 Activator WASH Controls the Fission of Endosomes through a Large Multiprotein Complex
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Regulation of branched F-actin formation by WASH is needed for proper morphology of the endolysosomal system and endosomal trafficking of a broad range of cargoes.
“Regulation of branched F-actin formation by WASH is needed for proper morphology of the endolysosomal system and endosomal trafficking of a broad range of cargoes37,39,41–44”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [37]
The Results show that blocking WASH-mediated Arp2/3 activation causes endosomal tubulation, and that WASH depletion impairs transferrin recycling. They do not establish defective trafficking of a broad range of cargoes or a requirement for normal morphology across the entire endolysosomal system; the LDL experiments track WASH localization rather than a trafficking defect. (LLM, conf=0.88)
Experimental — accuracy not yet measuredWASH complex is localised to endosomes via a retromer-independent mechanism that may rely on direct ability of WASH to bind lipids.
“From these data, we propose a working model (Figure 4H) where the WASH complex is localised to endosomes via a retromer-independent mechanism that may, in part, rely on the direct ability of the WASH complex to bind lipids21, 23.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [23]
The Results (page unavailable) show that the purified WASH complex binds liposomes and suggest that direct interaction with endosomal lipids may partly explain its localization. The copy also establishes that WASH localizes to endosomes, but the retrieved passages do not establish that this localization is retromer-independent. (LLM, conf=0.86)
Experimental — accuracy not yet measuredMammalian cells lacking strumpellin have an increased number of SNX1- and VPS26-positive endosomal tubules.
“Mammalian cells lacking strumpellin have an increased number of SNX1- and VPS26-positive endosomal tubules [9,10,13].”
From The hereditary spastic paraplegia protein strumpellin: Characterisation in neurons and of the effect of disease mutations on WASH complex assembly and function (2013) · cites this paper as [9]
The Results (page unavailable) report more transferrin-positive endosomal tubules after WASH depletion and tubules after depletion of another WASH-complex subunit, KIAA1033. They identify KIAA0196 as a complex member, but do not report tubulation after its depletion or establish that the tubules are SNX1- and VPS26-positive. The specific strumpellin-depletion and marker claims are therefore unsupported by this paper. (LLM, conf=0.86)
Experimental — accuracy not yet measuredModels of the stoichiometry of the WASH complex suggest that there is 1 strumpellin molecule in the complex.
“Models of the stoichiometry of the WASH complex suggest that there is 1 strumpellin molecule in the complex [9,15].”
From The hereditary spastic paraplegia protein strumpellin: Characterisation in neurons and of the effect of disease mutations on WASH complex assembly and function (2013) · cites this paper as [9]
The Results (page unavailable) include KIAA0196 among the proposed WASH-complex subunits and say that a model with one of each subunit per complex already exceeds the measured mass. This supports the proposed one-per-complex stoichiometry, but our copy does not identify KIAA0196 as strumpellin, so the strumpellin-specific attribution cannot be verified from it. (LLM, conf=0.79)
Experimental — accuracy not yet measuredThe WASH complex functions in endocytic recycling, maintenance of endolysosomal network integrity, exocytosis, cell adhesion, and cell migration.
“The WASH complex functions in the endocytic recycling of various types of membrane proteins, maintenance of endolysosomal network integrity, exocytosis, cell adhesion, and cell migration (11-23).”
From Hereditary spastic paraplegia SPG8 mutations impair CAV1-dependent, integrin-mediated cell adhesion (2020) · cites this paper as [11]
The Results (page unavailable) show that WASH depletion impairs transferrin recycling and causes tubulation across several endosomal compartments, supporting a role in recycling and endosomal organization. Our copy does not establish recycling of various types of membrane proteins or functions in exocytosis, cell adhesion, or cell migration. (LLM, conf=0.88)
Experimental — accuracy not yet measured
WASH serves as an actin nucleation-promoting factor for the ARP2/3 complex, which drives the generation of branched F-actin filaments on endosomal membranes.
“WASH serves as an actin nucleation-promoting factor for the ARP2/3 complex, which drives the generation of branched F-actin filaments on endosomal membranes37–40”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [37]
WASH is recruited to endosomes where it is necessary for branched F-actin deposition, a process essential to maintain endolysosomal network structure, promote fission of membrane tubules, and traffic cargo proteins.
“WASH is recruited to endosomes where it is necessary for branched F-actin deposition, a process that is essential to maintain the structure of the endolysosomal network, to promote effective fission of membrane tubules and trafficking of cargo proteins37,39,41,43,44.”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [37]
WASH complex has inherent ability to bind phospholipids.
“While the mechanism for retromer-independent association of the WASH complex to endosomes remains to be established it is perhaps worth noting that the WASH complex has an inherent ability to bind to phospholipids21, 23.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [23]
The ten members of the COMMD protein family readily form heterodimers both in vitro and in cells through their conserved C-terminal COMM domains.
“The ten members of the COMMD protein family are known to readily form heterodimers both in vitro and in cells through their conserved C-terminal COMM domains15,17.”
From Structural organization of the retriever–CCC endosomal recycling complex (2024) · cites this paper as [15]
The Results and Discussion passages describe a heterodimer of capping protein (CP) associated with the WASH complex, not COMMD proteins. Searches for COMMD-family heterodimers and conserved C-terminal COMM domains found no passage addressing the attributed claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredStrumpellin is a component of the WASH complex.
“Strumpellin is a component of the WASH complex, an actin-regulating complex that is recruited to endosomes by interactions with the retromer complex.”
Cells lacking components of the WASH complex, including strumpellin, have increased endosomal tubulation.
“Thus cells lacking components of the WASH complex, including strumpellin, have increased endosomal tubulation, consistent with a defect in tubule fission from the endosome [9,10,13].”
Cells depleted of other WASH complex components, such as Wash1, also have increased endosomal tubulation.
“Cells depleted of other WASH complex components, such as Wash1, also have increased endosomal tubulation, and this phenotype has been interpreted as a consequence of the loss of a WASH complex-generated pushing force involved in endosomal tubule fission [9,10].”
The WASH complex has been implicated in activation of the Arp2/3 actin polymerization nucleator at endosomes, a process thought to precede dynamin-controlled endosomal fission.
“the Wiskott-Aldrich syndrome protein and SCAR homolog (WASH) complex has been implicated in activation of the Arp2/3 actin polymerization nucleator at endosomes, a process thought to precede dynamin-controlled endosomal fission”
From Sorting nexin 17 (SNX17) links endosomal sorting to Eps15 homology domain protein 1 (EHD1)–mediated fission machinery (2020) · cites this paper as [59]
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Metadata
- Authors
- Derivery, E., Sousa, C., Gautier, J. J., Lombard, B., Loew, D., & Gautreau, A.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2009-11
- Volume
- 17
- Issue
- 5
- Pages
- 712-723
- ISSN
- 1534-5807
- Cited by
- 602
- References
- 0
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1390 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Funders
- Agence Nationale pour le Développement de la Recherche en Santé (ANR-08-BLAN-0012-03, ANR-08-PCVI-0010-03)
- Centre Eau Terre Environnement, Institut National de la Recherche Scientifique
- Fondation pour la Recherche Médicale (INE20071110919)
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