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SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane

Lauffer, Benjamin E.L., Melero, Cristina, Temkin, Paul, Lei, Cai, Hong, Wanjin, Kortemme, Tanja, von Zastrow, Mark·2010·Journal of Cell Biology
DOI 10.1083/jcb.201004060PMC PMC2928020
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Abstract

Postsynaptic density 95/discs large/zonus occludens-1 (PDZ) domain–interacting motifs, in addition to their well-established roles in protein scaffolding at the cell surface, are proposed to act as cis-acting determinants directing the molecular sorting of transmembrane cargo from endosomes to the plasma membrane. This hypothesis requires the existence of a specific trans-acting PDZ protein that mediates the proposed sorting operation in the endosome membrane. Here, we show that sorting nexin 27 (SNX27) is required for efficient PDZ-directed recycling of the β2-adrenoreceptor (β2AR) from early endosomes. SNX27 mediates this sorting function when expressed at endogenous levels, and its recycling activity requires both PDZ domain–dependent recognition of the β2AR cytoplasmic tail and Phox homology (PX) domain–dependent association with the endosome membrane. These results identify a discrete role of SNX27 in PDZ-directed recycling of a physiologically important signaling receptor, and extend the concept of cargo-specific molecular sorting in the recycling pathway.

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Crossref · 10.1083/jcb.201004060

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  • 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 [26]

    The Introduction identifies SNX27 as a sorting nexin involved in PDZ-directed recycling, supporting its inclusion among sorting proteins. But the cited paper does not establish that SNX27 associates with Retromer; a search for “retromer” found no passage making that link. The other protein groups in the sentence have separate citations and are not attributed to this source. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • Through 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 [26]

    The Results and discussion section says SNX27-mediated recycling requires both PDZ-motif binding and association with the endosome membrane, and identifies SNX27 as a mediator of endosome-to-plasma-membrane sorting. It does not establish that SNX27 regulates hundreds of cargoes; the study focuses on β2AR, while noting other receptors with PDZ-dependent recycling. Page numbers are unavailable in our copy. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Through 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 [26]

    The Results and discussion show that the SNX27 PDZ domain binds a motif in the C-terminal tail of β2AR. Our copy does not establish that SNX27 also interacts with Retromer through that domain, or that the two interactions occur simultaneously. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

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Citations

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Metadata

Authors
Lauffer, B. E. L., Melero, C., Temkin, P., Lei, C., Hong, W., Kortemme, T., & von Zastrow, M.
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2010-08-23
Volume
190
Issue
4
Pages
565-574
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.201004060
PMC
PMC2928020
Cited by
260
References
2
Language
en

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