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      Retromer revisited: Evolving roles for retromer in endosomal sorting

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      Author(s): ,
      Publication date (Print):
      Journal: The Journal of Cell Biology
      Publisher: The Rockefeller University Press

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          Abstract

          Chamberland and Ritter discuss work from Kvainickas et al. and Simonetti et al. demonstrating a retromer-independent function of SNX-BAR proteins in endosomal recycling.

          Abstract

          The highly conserved retromer complex has been linked to cargo retrieval from endosomes to the trans-Golgi network. In this issue, Kvainickas et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201702137) and Simonetti et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201703015) fundamentally question the current retromer model and demonstrate that in mammalian cells, the individual retromer subcomplexes have functionally diverged to organize multiple distinct sorting pathways.

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          Chlamydia interfere with an interaction between the mannose-6-phosphate receptor and sorting nexins to counteract host restriction

          Cherilyn A. Elwell, Nadine Czudnochowski, John Von Dollen … (2017)
          Chlamydia trachomatis is an obligate intracellular pathogen that resides in a membrane-bound compartment, the inclusion. The bacteria secrete a unique class of proteins, Incs, which insert into the inclusion membrane and modulate the host-bacterium interface. We previously reported that IncE binds specifically to the Sorting Nexin 5 Phox domain (SNX5-PX) and disrupts retromer trafficking. Here, we present the crystal structure of the SNX5-PX:IncE complex, showing IncE bound to a unique and highly conserved hydrophobic groove on SNX5. Mutagenesis of the SNX5-PX:IncE binding surface disrupts a previously unsuspected interaction between SNX5 and the cation-independent mannose-6-phosphate receptor (CI-MPR). Addition of IncE peptide inhibits the interaction of CI-MPR with SNX5. Finally, C. trachomatis infection interferes with the SNX5:CI-MPR interaction, suggesting that IncE and CI-MPR are dependent on the same binding surface on SNX5. Our results provide new insights into retromer assembly and underscore the power of using pathogens to discover disease-related cell biology. DOI: http://dx.doi.org/10.7554/eLife.22709.001
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            SNX-1 and RME-8 oppose the assembly of HGRS-1/ESCRT-0 degradative microdomains on endosomes.

            Anne Norris, Prasad Tammineni, Simon Wang … (2017)
            After endocytosis, transmembrane cargo reaches endosomes, where it encounters complexes dedicated to opposing functions: recycling and degradation. Microdomains containing endosomal sorting complexes required for transport (ESCRT)-0 component Hrs [hepatocyte growth factor-regulated tyrosine kinase substrate (HGRS-1) in Caenorhabditis elegans] mediate cargo degradation, concentrating ubiquitinated cargo and organizing the activities of ESCRT. At the same time, retromer associated sorting nexin one (SNX-1) and its binding partner, J-domain protein RME-8, sort cargo away from degradation, promoting cargo recycling to the Golgi. Thus, we hypothesized that there could be important regulatory interactions between retromer and ESCRT that balance degradative and recycling functions. Taking advantage of the naturally large endosomes of the C. elegans coelomocyte, we visualized complementary ESCRT-0 and RME-8/SNX-1 microdomains in vivo and assayed the ability of retromer and ESCRT microdomains to regulate one another. We found in snx-1(0) and rme-8(ts) mutants increased endosomal coverage and intensity of HGRS-1-labeled microdomains, as well as increased total levels of HGRS-1 bound to membranes. These effects are specific to SNX-1 and RME-8, as loss of other retromer components SNX-3 and vacuolar protein sorting-associated protein 35 (VPS-35) did not affect HGRS-1 microdomains. Additionally, knockdown of hgrs-1 had little to no effect on SNX-1 and RME-8 microdomains, suggesting directionality to the interaction. Separation of the functionally distinct ESCRT-0 and SNX-1/RME-8 microdomains was also compromised in the absence of RME-8 and SNX-1, a phenomenon we observed to be conserved, as depletion of Snx1 and Snx2 in HeLa cells also led to greater overlap of Rme-8 and Hrs on endosomes.
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              Author and article information

              Journal
              Journal ID (nlm-ta): J Cell Biol
              Journal ID (iso-abbrev): J. Cell Biol
              Journal ID (publisher-id): jcb
              Journal ID (hwp): jcb
              Title: The Journal of Cell Biology
              Publisher: The Rockefeller University Press
              ISSN (Print): 0021-9525
              ISSN (Electronic): 1540-8140
              Publication date (Print): 06 November 2017
              Volume: 216
              Issue: 11
              Pages: 3433-3436
              Affiliations
              [1]Department of Biochemistry, Boston University School of Medicine, Boston, MA
              Author notes
              Correspondence to Brigitte Ritter: britter@ 123456bu.edu
              Author information
              http://orcid.org/0000-0002-0094-0460
              Article
              Publisher ID: 201708111
              DOI: 10.1083/jcb.201708111
              PMC ID: 5674901
              PubMed ID: 29061649
              SO-VID: bc7767ae-b0d9-4917-b839-ca8249e401ea
              Copyright © © 2017 Chamberland and Ritter
              License:

              This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

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              ScienceOpen disciplines: Cell biology
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              ScienceOpen disciplines: Cell biology

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