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Evidence for an Alternate Pathway for Lysosomal Enzyme Targeting (Oligosaccharides/Lysosomes/Phosphorylation) CHRISTOPHER A
Proc. NatL Acad. Sci. USA Vol. 80, pp. 775-779, February 1983 Cell Biology Identification and characterization of cells deficient in the mannose 6-phosphate receptor: Evidence for an alternate pathway for lysosomal enzyme targeting (oligosaccharides/lysosomes/phosphorylation) CHRISTOPHER A. GABEL, DANIEL E. GOLDBERG, AND STUART KORNFELD Departments of Internal Medicine and Biological Chemistry, Division of Hematology-Oncology, Washington University School of Medicine, St. Louis, Missouri 63110 Contributed by Stuart Kornfeld, November 3, 1982 ABSTRACT Newly synthesized lysosomal enzymes acquire dence that this cell line is deficient in Man-6-P receptor activity. phosphomannosyl units, which allow bindingofthe enzymes to the We also identify several additional cell lines that lack receptor mannose 6-phosphate receptor and subsequent translocation to activity yet possess high levels ofintracellular hydrolase activity. lysosomes. In some cell types, this sequence ofevents is necessary These data indicate that some cells possess pathways indepen- for the delivery ofthese enzymes to lysosomes. Using a slime mold dent of the Man-6-P receptor for the intracellular transport of lysosomal hydrolase as a probe, we have identified three murine acid hydrolases to lysosomes. cell lines that lack the receptor and one line that contains very low (3%) receptor activity. Each ofthese lines synthesizes the mannose MATERIALS AND METHODS 6-phosphate recognition marker on its lysosomal enzymes, but, Cells. BW5147 mouse lymphoma, P388D1 mouse macro- unlike cell lines with high levels of receptor, the cells accumulate MOPC 315 oligosaccharides containing phosphomonoesters. The receptor- phage, J774.2 mouse macrophage, mouse L cells, deficient lines possess high levels of intracellular acid hydrolase mouse myeloma, Chinese hamster ovary (CHO), and (human) activity, which is contained in dense granules characteristic of ly- HeLa cells were grown in suspension culture in a minimal es- sosomes. -
The Endomembrane System and Proteins
Chapter 4 | Cell Structure 121 Endosymbiosis We have mentioned that both mitochondria and chloroplasts contain DNA and ribosomes. Have you wondered why? Strong evidence points to endosymbiosis as the explanation. Symbiosis is a relationship in which organisms from two separate species depend on each other for their survival. Endosymbiosis (endo- = “within”) is a mutually beneficial relationship in which one organism lives inside the other. Endosymbiotic relationships abound in nature. We have already mentioned that microbes that produce vitamin K live inside the human gut. This relationship is beneficial for us because we are unable to synthesize vitamin K. It is also beneficial for the microbes because they are protected from other organisms and from drying out, and they receive abundant food from the environment of the large intestine. Scientists have long noticed that bacteria, mitochondria, and chloroplasts are similar in size. We also know that bacteria have DNA and ribosomes, just like mitochondria and chloroplasts. Scientists believe that host cells and bacteria formed an endosymbiotic relationship when the host cells ingested both aerobic and autotrophic bacteria (cyanobacteria) but did not destroy them. Through many millions of years of evolution, these ingested bacteria became more specialized in their functions, with the aerobic bacteria becoming mitochondria and the autotrophic bacteria becoming chloroplasts. The Central Vacuole Previously, we mentioned vacuoles as essential components of plant cells. If you look at Figure 4.8b, you will see that plant cells each have a large central vacuole that occupies most of the cell's area. The central vacuole plays a key role in regulating the cell’s concentration of water in changing environmental conditions. -
A Mitochondria–Lysosome Transport Pathway
RESEARCH HIGHLIGHTS Controlling enteric nerve Interestingly, inhibition of integrin signalling The authors used point mutations to establish cell migration or ROCK activity rescued directed migration of that residue Met 44 of actin was essential for the MEFs and normalized the migration of ENCCs F-actin-severing function of Mical. Manipulation A functional gastrointestinal system is in organ cultures. Although the precise function of Mical levels is known to generate abnormal dependent on the enteric nervous system, of Phactr4 remains to be discovered, these data bristle cell processes in Drosophila. In the present which is formed during embryogenesis through demonstrate its role in regulating lamellipodial study, mutation of the Met 44 actin residue colonization of the gut by enteric neural crest actin dynamics through cofilin activity suppressed Mical overexpression phenotypes cells (ENCCs). Now, Niswander and colleagues controlled by integrin and PP1 signalling. CKR and phenocopied Mical loss-of-function effects identify the protein phosphatase 1 (PP1)- and in Drosophila. Together, these findings establish actin-binding protein Phactr4 as a regulator actin as a direct substrate of Mical and reveal of directional and collective ENCC migration a specific oxidation-dependent mechanism (Genes Dev. 26, 69–81; 2012). Actin gets the oxidation to regulate actin filament dynamics and cell Analysis of mouse embryos expressing treatment from Mical processes in vivo. AIZ a Phactr4 mutation known to abolish PP1 binding revealed reduced enteric neuronal Mical, an enzyme mediating redox reactions, numbers and defective organization at is known to promote actin remodelling embryonic day 18.5, and reduced ENCC in response to semaphorin signalling by A mitochondria–lysosome numbers in the gut at earlier stages (E12.5). -
Reflux of Endoplasmic Reticulum Proteins to the Cytosol Yields Inactivation of Tumor Suppressors
bioRxiv preprint doi: https://doi.org/10.1101/2020.04.13.038935; this version posted April 13, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Reflux of Endoplasmic Reticulum proteins to the cytosol yields inactivation of tumor suppressors Daria Sicari1,2, Raphael Pineau1,2, Pierre-Jean Le Reste1,2,3, Luc Negroni4,5,6,7, Sophie Chat8, Aiman Mohtar9, Daniel Thomas8, Reynald Gillet8, M. Ted Hupp9,10, Eric Chevet1,2* and Aeid Igbaria1,2,11* 1Inserm U1242, University of Rennes, Rennes, France. 2Centre de lutte contre le cancer Eugène Marquis, Rennes, France. 3Neurosurgery Dept, University Hospital of Rennes, 35000 Rennes, France. 4Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France. 5Centre National de la Recherche Scientifique, UMR7104, 67404 Illkirch, France. 6Institut National de la Santé et de la Recherche Médicale, U1258, 67404 Illkirch, France. 7Université de Strasbourg, 67404 Illkirch, France. 8Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR6290, 35000 Rennes, France. 9Edinburgh Cancer Research Centre at the Institute of Genetics and Molecular Medicine, Edinburgh University, Edinburgh, UK. 10International Centre for Cancer Vaccine Science, Gdansk, Poland. 11Department of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva 8410501, Israel. *Correspondence: [email protected], or [email protected] ABSTRACT: In the past decades many studies reported Endoplasmic Reticulum (ER) resident proteins to localize to the cytosol but the mechanisms by which this occurs and whether these proteins exert cytosolic functions remain unknown. We found that select ER luminal proteins accumulate in the cytosol of glioblastoma cells isolated from mouse and human tumors. -
L Is for Lytic Granules: Lysosomes That Kill
Biochimica et Biophysica Acta 1401Ž. 1998 146±156 View metadata, citation and similar papers at core.ac.uk brought to you by CORE Review provided by Elsevier - Publisher Connector L is for lytic granules: lysosomes that kill Lesley J. Page 1, Alison J. Darmon 2, Ruth Uellner, Gillian M. Griffiths ) MRC Lab for Molecular Cell Biology, UniÕersity College London, Gower St, London WC1E 6BT, UK Received 23 June 1997; revised 30 October 1997; accepted 31 October 1997 Contents 1. Introduction ................................................... 147 2. CTL function and biochemistry ....................................... 147 2.1. The function of CTL .......................................... 147 2.2. Mechanisms of killing.......................................... 147 2.3. Cytolytic proteins ............................................ 148 2.4. Target cell death ............................................. 149 2.5. Serial killing ............................................... 150 3. The lytic granule as a lysosome ....................................... 150 3.1. Lysosomal contents ........................................... 150 3.2. Lytic granules are acidic compartments ............................... 150 3.3. The lytic granule as an endocytic compartment ........................... 151 4. Lytic granules as secretory organelles ................................... 152 4.1. Sorting of lysosomal proteins ..................................... 152 4.2. Sorting of granzymes and perforin .................................. 152 5. Secretory lysosomes -
ER-Phagy at a Glance Paolo Grumati1,*, Ivan Dikic1,2,‡ and Alexandra Stolz2,*
© 2018. Published by The Company of Biologists Ltd | Journal of Cell Science (2018) 131, jcs217364. doi:10.1242/jcs.217364 CELL SCIENCE AT A GLANCE ER-phagy at a glance Paolo Grumati1,*, Ivan Dikic1,2,‡ and Alexandra Stolz2,* ABSTRACT function in response to ER stress signals. This task sharing reflects Selective autophagy represents the major quality control mechanism the complexity of the ER in terms of biological functions and that ensures proper turnover of exhausted or harmful organelles, morphology. In this Cell Science at a Glance article and the among them the endoplasmic reticulum (ER), which is fragmented accompanying poster, we summarize the most recent findings and delivered to the lysosome for degradation via a specific type of about ER-phagy in yeast and in mammalian cells. autophagy called ER-phagy. The recent discovery of ER-resident KEY WORDS: Autophagy, CCPG1, FAM134B, RTN3, SEC62, proteins that bind to mammalian Atg8 proteins has revealed that the Endoplasmic reticulum selective elimination of ER involves different receptors that are specific for different ER subdomains or ER stresses. FAM134B (also known as RETREG1) and RTN3 are reticulon-type proteins that are Introduction able to remodel the ER network and ensure the basal membrane The endoplasmic reticulum (ER) is the largest membrane-bound turnover. SEC62 and CCPG1 are transmembrane ER receptors that organelle in eukaryotic cells. Its complex morphology, which involves sheets, tubules and matrices (Chen et al., 2013; Friedman and Voeltz, 2011; Nixon-Abell et al., 2016), mirrors its diverse roles 1Institute of Biochemistry II, Goethe University Frankfurt - Medical Faculty, in a variety of physiological processes including autophagy University Hospital, 60590 Frankfurt am Main, Germany. -
Endomembrane System
Cell Structure & Function Cell Theory Cells are fundamental to biology Cells are the basic living units within organisms (all chemical rxns. of life take place within cells) All organisms are made of cells Single-celled organisms (bacteria/protists) Multicellular organisms (plants/animals/fungi) Cell Structure & Function Basic Aspects of Cell Structure & Function Plasma membrane Lipid bilayer Proteins DNA-containing region Cytoplasm Eukaryotic v. Prokaryotic cells Prokaryotic v. Eukaryotic Cells Two major classes of cells Prokaryotic cells (pro-, “before”) Cell lacks a “true” nucleus DNA is coiled in a nucleoid region Cells lack nuclear membrane Prokaryotic v. Eukaryotic Cells [attachment structure] [DNA location] [organelles that synthesize proteins] [enclosing the cytoplasm] [rigid structure outside the p.m. ] [jelly-like outer coating] [locomotion organelle] Prokaryotic v. Eukaryotic Cells Eukaryotic cells (eu-, “true”) Nucleus contains most of the cells nuclear material, DNA usually the largest organelle Bordered by a membranous envelope Prokaryotic v. Eukaryotic Cells Plant v. Animal Cells Both contain Plasma membrane (functions as a selective barrier) Nucleus (gene-containing organelle) Cytoplasm (region between nucleus and p.m.) Consists of organelles in a fluid (cytosol) Prokaryotic v. Eukaryotic Cells Plant v. Animal Cells Organelles Bordered by internal membranes Compartmentalizes the functions of a cell Maintains organelle’s unique environment Most organelles are found in both plant and animal cells Plant v. Animal Cells -
ER-Phagy and Its Role in ER Homeostasis in Plants
plants Review ER-Phagy and Its Role in ER Homeostasis in Plants Yan Bao 1,2,* and Diane C. Bassham 1,* 1 Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011, USA 2 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA * Correspondence: [email protected] (Y.B.); [email protected] (D.C.B.) Received: 19 November 2020; Accepted: 11 December 2020; Published: 14 December 2020 Abstract: The endoplasmic reticulum (ER) is the largest continuous membrane-bound cellular organelle and plays a central role in the biosynthesis of lipids and proteins and their distribution to other organelles. Autophagy is a conserved process that is required for recycling unwanted cellular components. Recent studies have implicated the ER as a membrane source for the formation of autophagosomes, vesicles that transport material to the vacuole during autophagy. When unfolded proteins accumulate in the ER and/or the ER lipid bilayer is disrupted, a condition known as ER stress results. During ER stress, ER membranes can also be engulfed through autophagy in a process termed ER-phagy. An interplay between ER stress responses and autophagy thus maintains the functions of the ER to allow cellular survival. In this review, we discuss recent progress in understanding ER-phagy in plants, including identification of regulatory factors and selective autophagy receptors. We also identify key unanswered questions in plant ER-phagy for future study. Keywords: autophagy; endoplasmic reticulum; ER stress; ER-phagy; unfolded protein response 1. Introduction Plants live in a world of ever-changing conditions; for survival, they need to adapt to the challenges of their surroundings to balance growth and stress responses [1,2]. -
And Cytosolic Proteases Endoplasmic Reticulum Aminopeptidase 1
Processing of a Class I-Restricted Epitope from Tyrosinase Requires Peptide N -Glycanase and the Cooperative Action of Endoplasmic Reticulum Aminopeptidase 1 This information is current as and Cytosolic Proteases of September 28, 2021. Michelle L. Altrich-VanLith, Marina Ostankovitch, Joy M. Polefrone, Claudio A. Mosse, Jeffrey Shabanowitz, Donald F. Hunt and Victor H. Engelhard J Immunol 2006; 177:5440-5450; ; Downloaded from doi: 10.4049/jimmunol.177.8.5440 http://www.jimmunol.org/content/177/8/5440 http://www.jimmunol.org/ References This article cites 45 articles, 25 of which you can access for free at: http://www.jimmunol.org/content/177/8/5440.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on September 28, 2021 • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2006 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Processing of a Class I-Restricted Epitope from Tyrosinase Requires Peptide N-Glycanase and the Cooperative Action of Endoplasmic Reticulum Aminopeptidase 1 and Cytosolic Proteases1 Michelle L. -
A Signal-Anchor Sequence Stimulates Signal Recognition Particle Binding to Ribosomes from Inside the Exit Tunnel
A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel Uta Berndta,b,1, Stefan Oellerera,b,c,1, Ying Zhanga,b,c, Arthur E. Johnsond, and Sabine Rosperta,b,2 aInstitute of Biochemistry and Molecular Biology and bCenter for Biological Signalling Studies, University of Freiburg, Stefan-Meier-Strasse 17, D-79104 Freiburg, Germany; cFakulta¨t fu¨ r Biologie, University of Freiburg, Scha¨nzlestrasse 1, D-79104 Freiburg, Germany; and dDepartment of Molecular and Cellular Medicine, Texas A&M Health Science Center, 116 Reynolds Medical Building, College Station, TX 77843 Edited by Arthur Horwich, Yale University School of Medicine, New Haven, CT, and approved December 15, 2008 (received for review August 29, 2008) Sorting of eukaryotic membrane and secretory proteins depends direct interaction between SRP and the nascent chain. Previous on recognition of ribosome-bound nascent chain signal sequences studies have addressed the question of whether or not specific by the signal recognition particle (SRP). The current model suggests amino acid sequences of segments inside the tunnel can further that the SRP cycle is initiated when a signal sequence emerges from the affinity of SRP for RNCs (9, 10). Because signal sequences the ribosomal tunnel and binds to SRP. Then elongation is slowed would be prime candidates for such effects, this possibility was until the SRP-bound ribosome–nascent chain complex (RNC) is tested in the eukaryotic system by using RNCs carrying prep- targeted to the SRP receptor in the endoplasmic reticulum (ER) rolactin, a secreted protein with a cleavable signal sequence. membrane. The RNC is then transferred to the translocon, SRP is However, when nascent preprolactin was too short to exit the released, and translation resumes. -
The Ins and Outs of Autophagic Ribosome Turnover
Biochemistry, Biophysics and Molecular Biology Publications Biochemistry, Biophysics and Molecular Biology 2019 The Ins and Outs of Autophagic Ribosome Turnover Zakayo Kazibwe Iowa State University, [email protected] Ang-Yu Liu Iowa State University, [email protected] Gustavo C. Macintosh Iowa State University, [email protected] Diane C. Bassham Iowa State University, [email protected] Follow this and additional works at: https://lib.dr.iastate.edu/bbmb_ag_pubs Part of the Cell and Developmental Biology Commons, Genetics Commons, and the Molecular Biology Commons The complete bibliographic information for this item can be found at https://lib.dr.iastate.edu/ bbmb_ag_pubs/260. For information on how to cite this item, please visit http://lib.dr.iastate.edu/howtocite.html. This Article is brought to you for free and open access by the Biochemistry, Biophysics and Molecular Biology at Iowa State University Digital Repository. It has been accepted for inclusion in Biochemistry, Biophysics and Molecular Biology Publications by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. The Ins and Outs of Autophagic Ribosome Turnover Abstract Ribosomes are essential for protein synthesis in all organisms and their biogenesis and number are tightly controlled to maintain homeostasis in changing environmental conditions. While ribosome assembly and quality control mechanisms have been extensively studied, our understanding of ribosome degradation is limited. In yeast or animal cells, ribosomes are degraded after transfer into the vacuole or lysosome by ribophagy or nonselective autophagy, and ribosomal RNA can also be transferred directly across the lysosomal membrane by RNautophagy. In plants, ribosomal RNA is degraded by the vacuolar T2 ribonuclease RNS2 after transport by autophagy-related mechanisms, although it is unknown if a selective ribophagy pathway exists in plants. -
Autophagy Is Activated for Cell Survival After Endoplasmic Reticulum Stress
University of Massachusetts Medical School eScholarship@UMMS Program in Gene Function and Expression Publications and Presentations Molecular, Cell and Cancer Biology 2006-10-13 Autophagy is activated for cell survival after endoplasmic reticulum stress Maiko Ogata University of Miyazaki Et al. Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/pgfe_pp Part of the Genetics and Genomics Commons Repository Citation Ogata M, Hino S, Saito A, Morikawa K, Kondo S, Kanemoto S, Murakami T, Taniguchi M, Tanii I, Yoshinaga K, Shiosaka S, Hammarback JA, Urano F, Imaizumi K. (2006). Autophagy is activated for cell survival after endoplasmic reticulum stress. Program in Gene Function and Expression Publications and Presentations. https://doi.org/10.1128/MCB.01453-06. Retrieved from https://escholarship.umassmed.edu/pgfe_pp/ 113 This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in Program in Gene Function and Expression Publications and Presentations by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. MOLECULAR AND CELLULAR BIOLOGY, Dec. 2006, p. 9220–9231 Vol. 26, No. 24 0270-7306/06/$08.00ϩ0 doi:10.1128/MCB.01453-06 Copyright © 2006, American Society for Microbiology. All Rights Reserved. Autophagy Is Activated for Cell Survival after Endoplasmic Reticulum Stressᰔ Maiko Ogata,1,2† Shin-ichiro Hino,1† Atsushi Saito,1,2 Keisuke Morikawa,2 Shinichi Kondo,1 Soshi Kanemoto,1,2 Tomohiko Murakami,1,2 Manabu Taniguchi,3 Ichiro Tanii,1 Kazuya Yoshinaga,1 Sadao Shiosaka,2 James A.