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      Invisible leashes: The tethering VAPs from infectious diseases to neurodegeneration

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          Abstract

          Intracellular organelles do not, as thought for a long time, act in isolation but are dynamically tethered together by entire machines responsible for interorganelle trafficking and positioning. Among the proteins responsible for tethering is the family of VAMP-associated proteins (VAPs) that appear in all eukaryotes and are localized primarily in the endoplasmic reticulum. The major functional role of VAPs is to tether the endoplasmic reticulum with different organelles and regulate lipid metabolism and transport. VAPs have gained increasing attention because of their role in human pathology where they contribute to infections by viruses and bacteria and participate in neurodegeneration. In this review, we discuss the structure, evolution, and functions of VAPs, focusing more specifically on VAP-B for its relationship with amyotrophic lateral sclerosis and other neurodegenerative diseases.

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          A Completely Reimplemented MPI Bioinformatics Toolkit with a New HHpred Server at its Core.

          Andrei Lupas, Jonas Kübler, Vikram Alva … (2017)
          The MPI Bioinformatics Toolkit (https://toolkit.tuebingen.mpg.de) is a free, one-stop web service for protein bioinformatic analysis. It currently offers 34 interconnected external and in-house tools, whose functionality covers sequence similarity searching, alignment construction, detection of sequence features, structure prediction, and sequence classification. This breadth has made the Toolkit an important resource for experimental biology and for teaching bioinformatic inquiry. Recently, we replaced the first version of the Toolkit, which was released in 2005 and had served around 2.5 million queries, with an entirely new version, focusing on improved features for the comprehensive analysis of proteins, as well as on promoting teaching. For instance, our popular remote homology detection server, HHpred, now allows pairwise comparison of two sequences or alignments and offers additional profile HMMs for several model organisms and domain databases. Here, we introduce the new version of our Toolkit and its application to the analysis of proteins.
          Article 0 comments Cited 758 times – based on 0 reviews     Review now
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            Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7–RILP–p150Glued and late endosome positioning

            Nuno Rocha-Pereira, Coenraad Kuijl, Rik van der Kant … (2009)
            Late endosomes (LEs) have characteristic intracellular distributions determined by their interactions with various motor proteins. Motor proteins associated to the dynactin subunit p150Glued bind to LEs via the Rab7 effector Rab7-interacting lysosomal protein (RILP) in association with the oxysterol-binding protein ORP1L. We found that cholesterol levels in LEs are sensed by ORP1L and are lower in peripheral vesicles. Under low cholesterol conditions, ORP1L conformation induces the formation of endoplasmic reticulum (ER)–LE membrane contact sites. At these sites, the ER protein VAP (VAMP [vesicle-associated membrane protein]-associated ER protein) can interact in trans with the Rab7–RILP complex to remove p150Glued and associated motors. LEs then move to the microtubule plus end. Under high cholesterol conditions, as in Niemann-Pick type C disease, this process is prevented, and LEs accumulate at the microtubule minus end as the result of dynein motor activity. These data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells.
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              Structure and function of ER membrane contact sites with other organelles.

              Melissa Phillips, Gia Voeltz (2016)
              The endoplasmic reticulum (ER) is the largest organelle in the cell, and its functions have been studied for decades. The past several years have provided novel insights into the existence of distinct domains between the ER and other organelles, known as membrane contact sites (MCSs). At these contact sites, organelle membranes are closely apposed and tethered, but do not fuse. Here, various protein complexes can work in concert to perform specialized functions such as binding, sensing and transferring molecules, as well as engaging in organelle biogenesis and dynamics. This Review describes the structure and functions of MCSs, primarily focusing on contacts of the ER with mitochondria and endosomes.
              Article 0 comments Cited 213 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Annalisa Pastore
                Journal
                Journal ID (nlm-ta): J Biol Chem
                Journal ID (iso-abbrev): J Biol Chem
                Title: The Journal of Biological Chemistry
                Publisher: American Society for Biochemistry and Molecular Biology
                ISSN (Print): 0021-9258
                ISSN (Electronic): 1083-351X
                Publication date PMC-release: 18 February 2021
                Publication date Collection: 2021
                Publication date (Electronic): 18 February 2021
                Volume: 296
                Electronic Location Identifier: 100421
                Affiliations
                [1 ]UK Dementia Research Institute at King’s College London, The Maurice Wohl Institute, London, UK
                [2 ]Centre for Molecular and Biomolecular Informatics (CMBI), Radboud University Medical Centre, GA Nijmegen, Netherlands
                [3 ]Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA
                Author notes
                [∗ ]For correspondence: Annalisa Pastore annalisa.pastore@ 123456crick.ac.uk
                Article
                Publisher Item ID: S0021-9258(21)00194-0 Publisher ID: 100421
                DOI: 10.1016/j.jbc.2021.100421
                PMC ID: 8005810
                PubMed ID: 33609524
                SO-VID: 14841386-d3f5-4971-9dce-33f1e2c3fab7
                Copyright © © 2021 The Authors
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 22 December 2020
                Date revision received : 11 February 2021
                Categories
                Subject: JBC Reviews

                ScienceOpen disciplines: Biochemistry
                Keywords: als,endoplasmic reticulum,tethering proteins,vamp,ad, alzheimer's disease,als, amyotrophic lateral sclerosis,er, endoplasmic reticulum,fus, fused in sarcoma/translocated in liposarcoma protein,hcv, hepatitis c virus,ig, immunoglobulin,msp, major sperm protein,nsps, nonstructural proteins,pd, parkinson's disease,pdb, protein data bank,tdp-43, transactive response dna binding protein 43 kda,vap, vamp-associated protein
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: als, endoplasmic reticulum, tethering proteins, vamp, ad, alzheimer's disease, als, amyotrophic lateral sclerosis, er, endoplasmic reticulum, fus, fused in sarcoma/translocated in liposarcoma protein, hcv, hepatitis c virus, ig, immunoglobulin, msp, major sperm protein, nsps, nonstructural proteins, pd, parkinson's disease, pdb, protein data bank, tdp-43, transactive response dna binding protein 43 kda, vap, vamp-associated protein

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