HRS–WASH axis governs actin-mediated endosomal recycling and cell invasion

MacDonald, Ewan; Brown, Louise; Selvais, Arnaud; Liu, Han; Waring, Thomas; Newman, D; Bithell, Jessica; Grimes, Douglas; Urbé, Sylvie; Clague, Michael J.; Zech, Tobias

doi:10.1083/jcb.201710051

Cited by 50 publications

(59 citation statements)

References 71 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Recent studies demonstrate that the WASH complex also functions to orchestrate retromer-independent trafficking, by cooperating with retriever and the CCC complex (McNally et al, 2017). In addition to retromer, HRS (hepatocyte growth factorregulated tyrosine kinase substrate) also plays a role in regulating endosomal localization of WASH, although it is unclear whether the interaction between WASH and HRS is direct (MacDonald et al, 2018). It is reported that WASH and HRS cooperate to regulate endosomal recycling of epidermal growth factor receptor and the matrix metalloproteinase MT1-MMP (MacDonald et al, 2018).…”

Section: Wash Complexmentioning

confidence: 99%

“…In addition to retromer, HRS (hepatocyte growth factorregulated tyrosine kinase substrate) also plays a role in regulating endosomal localization of WASH, although it is unclear whether the interaction between WASH and HRS is direct (MacDonald et al, 2018). It is reported that WASH and HRS cooperate to regulate endosomal recycling of epidermal growth factor receptor and the matrix metalloproteinase MT1-MMP (MacDonald et al, 2018). The WASH complex also associates with BLOC-1 (biogenesis of lysosomal organelles complex-1), and may play a role in the formation of melanosomes (Monfregola et al, 2010;Ryder et al, 2013).…”

Section: Wash Complexmentioning

confidence: 99%

See 1 more Smart Citation

Endosome-to-TGN Trafficking: Organelle-Vesicle and Organelle-Organelle Interactions

Zhao

Billadeau

et al. 2020

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

Retrograde transport from endosomes to the trans-Golgi network (TGN) diverts proteins and lipids away from lysosomal degradation. It is essential for maintaining cellular homeostasis and signaling. In recent years, significant advancements have been made in understanding this classical pathway, revealing new insights into multiple steps of vesicular trafficking as well as critical roles of ER-endosome contacts for endosomal trafficking. In this review, we summarize up-to-date knowledge about this trafficking pathway, in particular, mechanisms of cargo recognition at endosomes and vesicle tethering at the TGN, and contributions of ER-endosome contacts.

show abstract

Section: Wash Complexmentioning

confidence: 99%

Section: Wash Complexmentioning

confidence: 99%

Endosome-to-TGN Trafficking: Organelle-Vesicle and Organelle-Organelle Interactions

Zhao

Billadeau

et al. 2020

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

show abstract

“…(A) Activation of Rab10 and then Rab8a/b by unknown guanine nucleotide exchange factors (GEFs) promotes their association with budding tubules, which originate in the perinuclear region of cells and could be described as a subset of tubular endosomes. Cargo selection proceeds by an unknown mechanism, which may be related to a specific lipid environment such as an enrichment in PI(4,5)P 2 or cholesterol (Ling et al, 2007;Tan et al, 2015;Annabi et al, 2001;Seveau et al, 2004), partitioning in highly curved membranes, direct binding of Rabs or adapters (Ling et al, 2007;Lock and Stow, 2005;Lau and Mruk, 2003), and/or cytoskeletal retention (MacDonald et al, 2018). (B) GTP-bound Rab10 and Rab8a/b recruit and activate MICAL1, which may bind two Rabs simultaneously (Rai et al, 2016;Esposito et al, 2018).…”

Section: Cloningmentioning

confidence: 99%

GRAF2, WDR44, and MICAL1 mediate Rab8/10/11–dependent export of E-cadherin, MMP14, and CFTR ΔF508

Häsler

Vallis

Pasche

et al. 2020

Journal of Cell Biology

View full text Add to dashboard Cite

In addition to the classical pathway of secretion, some transmembrane proteins reach the plasma membrane through alternative routes. Several proteins transit through endosomes and are exported in a Rab8-, Rab10-, and/or Rab11-dependent manner. GRAFs are membrane-binding proteins associated with tubules and vesicles. We found extensive colocalization of GRAF1b/2 with Rab8a/b and partial with Rab10. We identified MICAL1 and WDR44 as direct GRAF-binding partners. MICAL1 links GRAF1b/2 to Rab8a/b and Rab10, and WDR44 binds Rab11. Endogenous WDR44 labels a subset of tubular endosomes, which are closely aligned with the ER via binding to VAPA/B. With its BAR domain, GRAF2 can tubulate membranes, and in its absence WDR44 tubules are not observed. We show that GRAF2 and WDR44 are essential for the export of neosynthesized E-cadherin, MMP14, and CFTR ΔF508, three proteins whose exocytosis is sensitive to ER stress. Overexpression of dominant negative mutants of GRAF1/2, WDR44, and MICAL1 also interferes with it, facilitating future studies of Rab8/10/11–dependent exocytic pathways of central importance in biology.

show abstract

“…In addition, several proteins such as INCENP, PRC1, IFT27, and BBS6 that are involved in the formation or maintenance of cilia are localized to the midbody and the cytokinetic furrow and play a role for cytokinesis. 54 The interaction between CHMP4B and actin filaments shown here suggests that CHMP4B functions in collaboration with actin filaments to regulate the elongation and structural integrity of cilia. Several membrane curvature-related proteins have been shown to interact with the actin cytoskeleton.…”

Section: Discussionmentioning

confidence: 77%

ESCRT subunit CHMP4B localizes to primary cilia and is required for the structural integrity of the ciliary membrane

et al. 2019

View full text Add to dashboard Cite

Proteins specialized in the detection, generation, or stabilization of membrane curvature play important roles in establishing various morphologies of cells and cellular organelles. Primary cilia are cellular organelles that protrude from the cell surface using a microtubule-based cytoskeleton called the axoneme as a structural support.It is unclear whether the integrity of the high curvature of the ciliary membrane depends on membrane curvature-related proteins. Charged Multivesicular Body Protein 4B (CHMP4B), a subunit of the endosomal sorting complexes required for transport (ESCRT), can stabilize membrane curvature. Here we show that CHMP4B is involved in the assembly and maintenance of primary cilia. CHMP4B was localized to primary cilia in mammalian cells. Knockdown of CHMP4B interfered with cilium assembly and also caused fragmentation of preexisting cilia. By contrast, cilium formation was unaffected by the interruption of the ESCRT-dependent endocytic degradation pathway. Morpholino (MO)-mediated CHMP4B depletion in zebrafish embryos induced characteristic phenotypes of ciliary defects such as curved body axis, hydrocephalus, otolith malformation, and kidney cyst. Our study reveals a new role for the multifunctional protein CHMP4B as a key factor in maintaining the structural integrity of primary cilia. K E Y W O R D Sciliopathy phenotype, endosomal sorting complex, membrane curvature 1332 | JUNG et al.

show abstract

HRS–WASH axis governs actin-mediated endosomal recycling and cell invasion

Cited by 50 publications

References 71 publications

Endosome-to-TGN Trafficking: Organelle-Vesicle and Organelle-Organelle Interactions

Endosome-to-TGN Trafficking: Organelle-Vesicle and Organelle-Organelle Interactions

GRAF2, WDR44, and MICAL1 mediate Rab8/10/11–dependent export of E-cadherin, MMP14, and CFTR ΔF508

ESCRT subunit CHMP4B localizes to primary cilia and is required for the structural integrity of the ciliary membrane

Contact Info

Product

Resources

About