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      The emerging role of sorting nexins in cardiovascular diseases

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          Abstract

          The sorting nexin (SNX) family consists of a diverse group of cytoplasmic- and membrane-associated phosphoinositide-binding proteins that play pivotal roles in the regulation of protein trafficking. This includes the entire endocytic pathway, such as endocytosis, endosomal sorting, and endosomal signaling. Dysfunctions of SNX pathway are involved in several forms of cardiovascular disease (CVD). Moreover, SNX gene variants are associated with CVDs. In this review, we discuss the current knowledge on SNX-mediated regulatory mechanisms and their roles in the pathogenesis and treatment of CVDs.

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          Endosomal sorting and signalling: an emerging role for sorting nexins.

          Peter J. Cullen (2008)
          The endocytic network comprises a series of interconnected tubulo-vesicular membranous compartments that together regulate various sorting and signalling events. Although it is clear that defects in endocytic function underlie a variety of human diseases, our understanding of the molecular entities that regulate these sorting and signalling events remains limited. Here we discuss the sorting nexins family of proteins and propose that they have a fundamental role in orchestrating the formation of protein complexes that are involved in endosomal sorting and signalling.
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            Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease.

            Leonard Collins, M. D. Teasdale (2012)
            The mammalian genome encodes 49 proteins that possess a PX (phox-homology) domain, responsible for membrane attachment to organelles of the secretory and endocytic system via binding of phosphoinositide lipids. The PX domain proteins, most of which are classified as SNXs (sorting nexins), constitute an extremely diverse family of molecules that play varied roles in membrane trafficking, cell signalling, membrane remodelling and organelle motility. In the present review, we present an overview of the family, incorporating recent functional and structural insights, and propose an updated classification of the proteins into distinct subfamilies on the basis of these insights. Almost all PX domain proteins bind PtdIns3P and are recruited to early endosomal membranes. Although other specificities and localizations have been reported for a select few family members, the molecular basis for binding to other lipids is still not clear. The PX domain is also emerging as an important protein-protein interaction domain, binding endocytic and exocytic machinery, transmembrane proteins and many other molecules. A comprehensive survey of the molecular interactions governed by PX proteins highlights the functional diversity of the family as trafficking cargo adaptors and membrane-associated scaffolds regulating cell signalling. Finally, we examine the mounting evidence linking PX proteins to different disorders, in particular focusing on their emerging importance in both pathogen invasion and amyloid production in Alzheimer's disease.
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              Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B.

              Harald Stenmark, Anja Runge, Alicia Cabezas … (2005)
              Different classes of endosomes exhibit a characteristic intracellular steady-state distribution governed by interactions with the cytoskeleton. We found a kinesin-3, KIF16B, that transports early endosomes to the plus end of microtubules in a process regulated by the small GTPase Rab5 and its effector, the phosphatidylinositol-3-OH kinase hVPS34. In vivo, KIF16B overexpression relocated early endosomes to the cell periphery and inhibited transport to the degradative pathway. Conversely, expression of dominant-negative mutants or ablation of KIF16B by RNAi caused the clustering of early endosomes to the perinuclear region, delayed receptor recycling to the plasma membrane, and accelerated degradation. These results suggest that KIF16B, by regulating the plus end motility of early endosomes, modulates the intracellular localization of early endosomes and the balance between receptor recycling and degradation. We propose that this mechanism could have important implications for signaling.
              Article 0 comments Cited 81 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Clin Sci (Lond)
                Journal ID (iso-abbrev): Clin. Sci
                Journal ID (hwp): ppclinsci
                Journal ID (publisher-id): CS
                Title: Clinical Science (London, England : 1979)
                Publisher: Portland Press Ltd.
                ISSN (Print): 0143-5221
                ISSN (Electronic): 1470-8736
                Publication date Collection: 29 March 2019
                Publication date (Electronic): 15 March 2019
                Volume: 133
                Issue: 5
                Pages: 723-737
                Affiliations
                [1 ]Department of Clinical Nutrition, The Third Affiliated Hospital of Chongqing Medical University, Chongqing 410020, P.R. China
                [2 ]Department of Cardiology, Daping Hospital, The Third Military Medical University, Chongqing 400042, P.R. China
                [3 ]Division of Renal Diseases and Hypertension, Department of Medicine, and Department of Pharmacology/Physiology, The George Washington University School of Medicine and Health Sciences, Washington, DC 20052, U.S.A.
                Author notes
                Correspondence: Jian Yang ( jianyang@ 123456hospital.cqmu.edu.cn ) or Chunyu Zeng ( chunyuzeng01@ 123456163.com )
                Author information
                http://orcid.org/0000-0003-0173-5028
                Article
                DOI: 10.1042/CS20190034
                PMC ID: 6418407
                PubMed ID: 30877150
                SO-VID: 8284c2c3-2e50-4d0b-9b68-864bbad27dea
                Copyright © © 2019 The Author(s).
                License:

                This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND).

                History
                Date received : 14 January 2019
                Date revision received : 19 February 2019
                Date accepted : 28 February 2019
                Page count
                Pages: 15
                Categories
                Subject: Review Articles
                Subject: Review Article
                Subject: 40
                Subject: 10
                Subject: 13

                ScienceOpen disciplines: Medicine
                Keywords: cardiovascular diseases,endosomal sorting,pharmacogenomics,retromer,sorting nexin
                Data availability:
                ScienceOpen disciplines: Medicine
                Keywords: cardiovascular diseases, endosomal sorting, pharmacogenomics, retromer, sorting nexin

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