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SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
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Specific endosomal membrane sub-domains are enriched for either degradative components such as ESCRT or recycling machinery including Retromer, Retriever, the CCC complex, and WASH-dependent actin patches.
“A number of studies have shown that specific endosomal membrane sub-domains are enriched for either degradative components such as ESCRT or recycling machinery including Retromer, Retriever, the CCC complex, and WASH-dependent actin patches9,34–44”
From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [35]
The paper reports SNX1 and SNX5 enrichment on endosomal tubules associated with retromer and links SNX27 to the WASH actin-nucleation complex (Abstract section; page unavailable). It does not establish the claimed enrichment of ESCRT, Retriever, or the CCC complex in distinct endosomal sub-domains, or directly show WASH-dependent actin patches there. (LLM, conf=0.87)
Experimental — accuracy not yet measuredThrough this dual interaction SNX27 regulates the retrieval and recycling of hundreds of cargoes to the plasma membrane.
“Through this dual interaction SNX27 regulates the retrieval and recycling of hundreds of cargoes to the plasma membrane [26,29,31,58,59].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [31]
In the passage labelled Abstract (page unavailable), the paper reports that SNX27 binds a receptor’s PDZ motif and associates with retromer tubules through the WASH complex, promoting recycling to the plasma membrane. It demonstrates this pathway for β2AR and β1AR and suggests that many other cargoes may use it; it does not establish that SNX27 regulates hundreds of cargoes. (LLM, conf=0.89)
Experimental — accuracy not yet measuredSNX27 interacts with SNX-BAR proteins SNX1 and SNX2 and the WASH complex to couple sequence-dependent retrieval of SNX27 cargoes with tubule formation during cargo recycling.
“SNX27 also interacts with the SNX-BAR (Bin/Amphiphysin/Rvs) proteins SNX1 and SNX2 [27,28,31,62] and the WASH complex [37] to couple sequence-dependent retrieval of SNX27 cargoes with tubule formation during the process of cargo recycling.”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [31]
The paper reports that WASH-complex components co-purify with SNX27 and concludes that this connectivity helps SNX27 direct PDZ-dependent cargo sorting through retromer tubules (passage labeled Abstract; Fig. 5e–f). It supports the WASH interaction and sequence-dependent tubule entry, but does not establish that SNX27–WASH coupling drives tubule formation. The SNX1/SNX2 interaction is attached to other citations in the citing sentence. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThrough its PDZ domain, SNX27 can simultaneously interact with Retromer and cargoes containing a PDZ binding motif in their carboxy-terminal tail.
“Through its PDZ domain, SNX27 can simultaneously interact with Retromer and cargoes containing a PDZ binding motif (PDZbm) in their carboxy-terminal tail [26,29,31,57].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [31]
The passage discussing β2AR recycling says SNX27’s PDZ domain binds the receptor’s PDZ-containing tail. The passage discussing retromer-tubule association says SNX27 does not appear to interact directly with the retromer core; it proposes connectivity through the WASH complex instead. The paper therefore supports SNX27 linking cargo to retromer tubules, but not simultaneous binding of both through its PDZ domain. (LLM, conf=0.88)
Experimental — accuracy not yet measuredEndosomal retrieval and recycling is orchestrated through a specialised endosomal nanodomain, the retrieval sub-domain.
“and is orchestrated through a specialised endosomal nanodomain, the retrieval sub-domain”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [9]
The paper’s main text (indexed under Abstract; page unavailable) shows that β2-adrenergic receptors enter retromer-associated endosomal tubules and describes those tubules as a multifunctional exit port for recycling. It does not identify a structure called the “retrieval sub-domain” or establish that this nanodomain orchestrates endosomal retrieval and recycling generally. (LLM, conf=0.85)
Experimental — accuracy not yet measured
These foci represent previously described retrieval sub-domains from where cargo-enriched transport carriers exit the endosome.
“These foci therefore represent the previously described retrieval sub-domains from where cargo-enriched transport carriers exit the endosome for transport to their destination9,34,35,39,41,49.”
From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [35]
Retromer associates with accessory proteins and cargo adaptors including sorting nexins, the WASH complex, RAB GTPase regulators including TBC1D5 and ANKRD27/VARP, and RME8.
“To function, Retromer associates with accessory proteins and cargo adaptors including sorting nexins (SNXs) [24][25][26][27][28][29][30][31][32][33][34], the WASH complex [35][36][37][38][39], RAB GTPase regulators including TBC1D5 and ANKRD27/VARP [40][41][42][43][44][45][46], and RME8 [47].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [31]
Endosomal cargo retrieval and recycling are orchestrated by several multi-protein assemblies including SNX27-Retromer and SNX3-Retromer, SNX17-Retriever and associated Commander super-assembly, the WASH complex and its regulatory MUST complex, and the SNX-BAR proteins and ESCPE-1.
“Orchestrating endosomal cargo retrieval and recycling are several multi-protein assemblies that include sorting nexin-27 (SNX27)-Retromer and SNX3-Retromer8–16, SNX17-Retriever and associated Commander super-assembly17–22, the branched F-actin polymerising WASH complex and its regulatory MAGE-L2/USP7/TRIM27 (MUST) complex23–25, and the SNX-BAR proteins and endosomal sorting complex required for ex”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [9]
The WASH complex is implicated in β2AR recycling as it interacts with SNX27, an adapter that links β2AR to retromer-positive tubules.
“The WASH complex is also implicated in β2AR recycling as it interacts with SNX27, an adapter that links β2AR to retromer-positive tubules [29].”
Retromer orchestrates the retrieval of hundreds of internalised cargo and promotes their recycling to the cell surface, with GLUT1 as a prototypical cargo.
“The principal role of retromer is therefore is to orchestrate the retrieval of hundreds of internalised cargo and to promote their recycling to the cell surface (Temkin et al., 2011; Steinberg et al., 2013).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Temkin et al., 2011
The study's data provide insight into the temporal dynamics of endosomal cargo sorting and support the established role of retromer in cell surface recycling.
“By visualising the sorting of endogenous GLUT1 and CI-MPR, our data provide insight into the temporal dynamics of endosomal cargo sorting and support the established role of retromer in cell surface recycling (Temkin et al., 2011; Steinberg et al., 2013).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Temkin et al., 2011
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Research works printed but not linked: 44
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Metadata
- Authors
- Temkin, P., Lauffer, B., Jäger, S., Cimermancic, P., Krogan, N. J., & von Zastrow, M.
- Venue
- Nature Cell Biology
- Published
- 2011-05-22
- Volume
- 13
- Issue
- 6
- Pages
- 715-721
- ISSN
- 1465-7392
- 1476-4679
- PMC
- PMC3113693
- Cited by
- 459
- References
- 0
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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