Mechanisms of Endocytosis
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Clathrin-Independent Pathways of Endocytosis
Downloaded from http://cshperspectives.cshlp.org/ on October 3, 2021 - Published by Cold Spring Harbor Laboratory Press Clathrin-Independent Pathways of Endocytosis Satyajit Mayor1, Robert G. Parton2, and Julie G. Donaldson3 1National Centre for Biological Sciences, Tata Institute of Fundamental Research, and Institute for Stem Cell Biology and Regenerative Medicine, Bangalore 560065, India 2The University of Queensland, Institute for Molecular Bioscience and Centre for Microscopy and Microanalysis, Queensland 4072, Brisbane, Australia 3Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 Correspondence: [email protected] There are many pathways of endocytosis at the cell surface that apparently operate at the same time. With the advent of new molecular genetic and imaging tools, an understanding of the different ways by which a cell may endocytose cargo is increasing by leaps and bounds. In this review we explore pathways of endocytosis that occur in the absence of clathrin. These are referred to as clathrin-independent endocytosis (CIE). Here we primarily focus on those pathways that function at the small scale in which some have distinct coats (caveolae) and others function in the absence of specific coated intermediates. We follow the trafficking itineraries of the material endocytosed by these pathways and finally discuss the functional roles that these pathways play in cell and tissue physiology. It is likely that these pathways will play key roles in the regulation of plasma membrane area and tension and also control the availability of membrane during cell migration. he identification of many of the components Consequently, CME has remained a pre- Tinvolved in clathrin-mediated endocytosis dominant paradigm for following the uptake (CME) and their subsequent characterization of material into the cell. -
Variable Priming of a Docked Synaptic Vesicle PNAS PLUS
Variable priming of a docked synaptic vesicle PNAS PLUS Jae Hoon Junga,b,c, Joseph A. Szulea,c, Robert M. Marshalla,c, and Uel J. McMahana,c,1 aDepartment of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305; bDepartment of Physics, Stanford University School of Humanities and Sciences, Stanford, CA 94305; and cDepartment of Biology, Texas A&M University, College Station, TX 77845 Edited by Thomas S. Reese, National Institutes of Health, Bethesda, MD, and approved January 12, 2016 (received for review November 30, 2015) The priming of a docked synaptic vesicle determines the proba- transition. Biochemical and electrophysiological approaches have bility of its membrane (VM) fusing with the presynaptic membrane provided evidence that priming is mediated by interactions be- (PM) when a nerve impulse arrives. To gain insight into the nature tween the SNARE proteins and their regulators (7, 12–14, 24) and of priming, we searched by electron tomography for structural can involve differences in positioning of docked SVs relative to + relationships correlated with fusion probability at active zones of Ca2 channels (25). Biochemistry has also led to the suggestion axon terminals at frog neuromuscular junctions. For terminals that primed SVs may become deprimed (26). fixed at rest, the contact area between the VM of docked vesicles We have previously shown by electron tomography on frog and PM varied >10-fold with a normal distribution. There was no neuromuscular junctions (NMJs) fixed at rest that there are, for merging of the membranes. For terminals fixed during repetitive docked SVs, variations in the extent of the VM–PM contact area evoked synaptic transmission, the normal distribution of contact and in the length of the several AZM macromolecules linking areas was shifted to the left, due in part to a decreased number of the VM to the PM, the so-called ribs, pegs, and pins (2, 27). -
Mechanisms of Synaptic Plasticity Mediated by Clathrin Adaptor-Protein Complexes 1 and 2 in Mice
Mechanisms of synaptic plasticity mediated by Clathrin Adaptor-protein complexes 1 and 2 in mice Dissertation for the award of the degree “Doctor rerum naturalium” at the Georg-August-University Göttingen within the doctoral program “Molecular Biology of Cells” of the Georg-August University School of Science (GAUSS) Submitted by Ratnakar Mishra Born in Birpur, Bihar, India Göttingen, Germany 2019 1 Members of the Thesis Committee Prof. Dr. Peter Schu Institute for Cellular Biochemistry, (Supervisor and first referee) University Medical Center Göttingen, Germany Dr. Hans Dieter Schmitt Neurobiology, Max Planck Institute (Second referee) for Biophysical Chemistry, Göttingen, Germany Prof. Dr. med. Thomas A. Bayer Division of Molecular Psychiatry, University Medical Center, Göttingen, Germany Additional Members of the Examination Board Prof. Dr. Silvio O. Rizzoli Department of Neuro-and Sensory Physiology, University Medical Center Göttingen, Germany Dr. Roland Dosch Institute of Developmental Biochemistry, University Medical Center Göttingen, Germany Prof. Dr. med. Martin Oppermann Institute of Cellular and Molecular Immunology, University Medical Center, Göttingen, Germany Date of oral examination: 14th may 2019 2 Table of Contents List of abbreviations ................................................................................. 5 Abstract ................................................................................................... 7 Chapter 1: Introduction ............................................................................ -
Palmitoylation: Implications for Nitric Oxide Signaling
Proc. Natl. Acad. Sci. USA Vol. 93, pp. 6448-6453, June 1996 Cell Biology Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling (endothelial nitric oxide synthase/signal transduction/vascular biology/N-myristoylation) GUILLERMO GARC1A-CARDENA*, PHIL OHt, JIANwEI LIu*, JAN E. SCHNITZERt, AND WILLIAM C. SESSA*t *Molecular Cardiobiology Program and Department of Pharmacology, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536; and tDepartment of Pathology, Harvard Medical School, Beth Israel Hospital, 330 Brookline Avenue, Boston, MA 02215 Communicated by Vincent T. Marchesi, Yale Univeristy, New Haven, CT, March 13, 1996 (received for review February 5, 1996) ABSTRACT The membrane association of endothelial insoluble membranes (TIM), suggesting that caveolae are nitric oxide synthase (eNOS) plays an important role in the signal processing centers (2-11). Additionally, caveolae have biosynthesis of nitric oxide (NO) in vascular endothelium. been implicated in other important cellular functions, includ- Previously, we have shown that in cultured endothelial cells ing endocytosis, potocytosis, and transcytosis (12, 13). and in intact blood vessels, eNOS is found primarily in the Endothelial nitric oxide synthase (eNOS) is a peripheral perinuclear region of the cells and in discrete regions of the membrane protein that metabolizes L-arginine to nitric oxide plasma membrane, suggesting trafficking of the protein from (NO). NO is a short-lived free radical gas involved in diverse the Golgi to specialized plasma membrane structures. Here, physiological and pathological processes. Endothelial-derived we show that eNOS is found in Triton X-100-insoluble mem- NO is an important paracrine mediator of vascular smooth branes prepared from cultured bovine aortic endothelial cells muscle tone and is an inhibitor of leukocyte adhesion and and colocalizes with caveolin, a coat protein of caveolae, in platelet aggregation (14, 15). -
Identification of Caveolin and Caveolin-Related Proteins in the Brain
The Journal of Neuroscience, December 15, 1997, 17(24):9520–9535 Identification of Caveolin and Caveolin-Related Proteins in the Brain Patricia L. Cameron, Johnna W. Ruffin, Roni Bollag, Howard Rasmussen, and Richard S. Cameron Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, Georgia 30912-3175 Caveolae are 50–100 nm, nonclathrin-coated, flask-shaped brane. Immunoblot analyses demonstrate that detergent- plasma membrane microdomains that have been identified in insoluble complexes isolated from astrocytes are composed of most mammalian cell types, except lymphocytes and neurons. caveolin-1a, an identification verified by Northern blot analyses To date, multiple functions have been ascribed to caveolae, and by the cloning of a cDNA using reverse transcriptase-PCR including the compartmentalization of lipid and protein compo- amplification from total astrocyte RNA. Using a full-length nents that function in transmembrane signaling events, biosyn- caveolin-1 probe, Northern blot analyses suggest that the ex- thetic transport functions, endocytosis, potocytosis, and trans- pression of caveolin-1 may be regulated during brain develop- cytosis. Caveolin, a 21–24 kDa integral membrane protein, is ment. Immunoblot analyses of detergent-insoluble complexes the principal structural component of caveolae. We have initi- isolated from cerebral cortex and cerebellum identify two im- ated studies to examine the relationship of detergent-insoluble munoreactive polypeptides with apparent molecular weight and complexes identified -
Endothelial Plasmalemma Vesicle–Associated Protein Regulates the Homeostasis of Splenic Immature B Cells and B-1 B Cells
Endothelial Plasmalemma Vesicle−Associated Protein Regulates the Homeostasis of Splenic Immature B Cells and B-1 B Cells This information is current as Raul Elgueta, Dan Tse, Sophie J. Deharvengt, Marcus R. of September 26, 2021. Luciano, Catherine Carriere, Randolph J. Noelle and Radu V. Stan J Immunol 2016; 197:3970-3981; Prepublished online 14 October 2016; doi: 10.4049/jimmunol.1501859 Downloaded from http://www.jimmunol.org/content/197/10/3970 Supplementary http://www.jimmunol.org/content/suppl/2016/10/13/jimmunol.150185 Material 9.DCSupplemental http://www.jimmunol.org/ References This article cites 64 articles, 25 of which you can access for free at: http://www.jimmunol.org/content/197/10/3970.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on September 26, 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 © 2016 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Endothelial Plasmalemma Vesicle–Associated Protein Regulates the Homeostasis of Splenic Immature B Cells and B-1 B Cells Raul Elgueta,*,† Dan Tse,‡,1 Sophie J. -
Internalization of Lectins in Neuronal Gerl
INTERNALIZATION OF LECTINS IN NEURONAL GERL NICHOLAS K. GONATAS, SEUNG U. KIM, ANNA STIEBER, and STRATIS AVRAMEAS From the Division of Neuropathology, Department of Pathology, University of PennsylvaniaSchool of Medicine, Philadelphia, Pennsylvania 19174, and the Laboratory of Immunocytochemistry,Pasteur Institute, Paris, France ABSTRACT Conjugates of ricin agglutinin and phytohemagglutinin with horseradish peroxi- dase (HRP) were used for a cytochemical study of internalization of their plasma membrane "receptors" in cultured isolated mouse dorsal root ganglion neurons. Labeling of cells with lectin-HRP was done at 4~ and internalization was performed at 37~ in a culture medium free of lectin-HRP. 15-30 rain after incubation at 37~ lectin-HRP-receptor complexes were seen in vesicles or tubules located near the plasma membrane. After 1-3 h at 37~ lectin-HRP- receptor complexes accumulated in vesicles and tubules corresponding to acid phosphatase-rich vesicles and tubules (GERL) at the trans aspect of the Golgi apparatus. A few coated vesicles and probably some dense bodies contained HRP after 3-6 h of incubation at 37~ Soluble HRP was not endocytosed under the conditions of this experiment or when it was present in the incubation medium at 37~ Internalization of lectin-HRP-receptor conjugates was decreased or in- hibited by mitochondrial respiration inhibitors but not by cytochalasin B or colchicine. These studies indicate that lectin-labeled plasma membrane moieties of neurons are endocytosed primarily in elements of GERL. Considerable information concerning the mobility tors" for ricin (Ric) and phytohemagglutinin and distribution of plasma membrane proteins has (PHA) labeled with horseradish peroxidase been gained with the use of various ligands. -
Part III: Modeling Neurotransmission – a Cholinergic Synapse
Part III: Modeling Neurotransmission – A Cholinergic Synapse Operation of the nervous system is dependent on the flow of information through chains of neurons functionally connected by synapses. The neuron conducting impulses toward the synapse is the presynaptic neuron, and the neuron transmitting the signal away from the synapse is the postsynaptic neuron. Chemical synapses are specialized for release and reception of chemical neurotransmitters. For the most part, neurotransmitter receptors in the membrane of the postsynaptic cell are either 1.) channel-linked receptors, which mediate fast synaptic transmission, or 2.) G protein-linked receptors, which oversee slow synaptic responses. Channel-linked receptors are ligand-gated ion channels that interact directly with a neurotransmitter and are called ionotropic receptors. Alternatively, metabotropic receptors do not have a channel that opens or closes but rather, are linked to a G-protein. Once the neurotransmitter binds to the metabotropic receptor, the receptor activates the G-protein which, in turn, goes on to activate another molecule. 3a. Model the ionotropic cholinergic synapse shown below. Be sure to label all of the following: voltage-gated sodium channel, voltage-gated potassium channel, neurotransmitter, synaptic vesicle, presynaptic cell, postsynaptic cell, potassium leak channel, sodium-potassium pump, synaptic cleft, acetylcholine receptor, acetylcholinesterase, calcium channel. When a nerve impulse (action potential) reaches the axon terminal, it sets into motion a chain of events that triggers the release of neurotransmitter. You will next model the events of neurotransmission at a cholinergic synapse. Cholinergic synapses utilize acetylcholine as the chemical of neurotransmission. MSOE Center for BioMolecular Modeling Synapse Kit: Section 3-6 | 1 Step 1 - Action potential arrives at the Step 2 - Calcium channels open in the terminal end of the presynaptic cell. -
Endocytosis of Viruses and Bacteria
Downloaded from http://cshperspectives.cshlp.org/ on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Endocytosis of Viruses and Bacteria Pascale Cossart1 and Ari Helenius2 1Institut Pasteur, Unite´ des Interactions Bacte´ries-Cellules, Paris F-75015, France; INSERM U604, Paris F-75015, France; and INRA, USC2020, Paris F-75015, France 2Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland Correspondence: [email protected]; [email protected] Of the many pathogens that infect humans and animals, a large number use cells of the host organism as protected sites for replication. To reach the relevant intracellular compartments, they take advantage of the endocytosis machinery and exploit the network of endocytic organelles for penetration into the cytosol or as sites of replication. In this review, we discuss the endocytic entry processes used by viruses and bacteria and compare the strategies used by these dissimilar classes of pathogens. any of the most widespread and devastat- valuable insights into fundamental aspects of Ming diseases in humans and livestock are cell biology. caused by viruses and bacteria that enter cells for Here, we focus on the mechanisms by which replication. Being obligate intracellular para- viral and bacterial pathogens exploit the endo- sites, viruses have no choice. They must trans- cytosis machinery for host cell entry and rep- port their genome to the cytosol or nucleus of lication. Among recent reviews on this topic, infected cells to multiply and generate progeny. dedicated uniquely to either mammalian vi- Bacteria and eukaryotic parasites do have other ruses or bacterial pathogens, we recommend options; most of them can replicate on their the following: Cossart and Sansonetti (2004); own. -
Synaptic Vesicle Endocytosis
Downloaded from http://cshperspectives.cshlp.org/ on September 24, 2021 - Published by Cold Spring Harbor Laboratory Press Synaptic Vesicle Endocytosis Yasunori Saheki and Pietro De Camilli Department of Cell Biology, Howard Hughes Medical Institute and Program in Cellular Neuroscience, Neurodegeneration and Repair, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, Connecticut 06510 Correspondence: [email protected] Neurons can sustain high rates of synaptic transmission without exhausting their supply of synaptic vesicles. This property relies on a highly efficient local endocytic recycling of syn- aptic vesicle membranes, which can be reused for hundreds, possibly thousands, of exo- endocytic cycles. Morphological, physiological, molecular, and genetic studies over the last four decades have provided insight into the membrane traffic reactions that govern this recy- cling and its regulation. These studies have shown that synaptic vesicle endocytosis capital- izes on fundamental and general endocytic mechanisms but also involves neuron-specific adaptations of such mechanisms. Thus, investigations of these processes have advanced not only the field of synaptic transmission but also, more generally, the field of endocytosis. This article summarizes current information on synaptic vesicle endocytosis with an emphasis on the underlying molecular mechanisms and with a special focus on clathrin-mediated endocytosis, the predominant pathway of synaptic vesicle protein internalization. t synapses, the number of synaptic vesicles neuromuscular junctions in combination with Athat undergo exocytosis over a given time such tracers conclusively established the con- period can greatly exceed the supply of synaptic cept of synaptic vesicle recycling (Ceccarelli vesicle precursors delivered from the cell body. et al. 1973; Heuser and Reese 1973). -
Review Caveolae: Where Incoming and Outgoing Messengers Meet Richard G
Proc. Natl. Acad. Sci. USA Vol. 90, pp. 10909-10913, December 1993 Review Caveolae: Where incoming and outgoing messengers meet Richard G. W. Anderson Department of Cell Biology and Neuroscience, University of Texas Southwestem Medical Center, Dallas, TX 75235 ABSTIRACT Plasmalemmal caveolae ing. At the same time, this information is This portable, membrane-bound com- were flrst identified as an endocytic com- used to construct several models that partment has been found to contain a partment In endothelial cells, where they illustrate the different ways that caveolae number of molecules that are known to appear to move molecules across the cell might function in both intracellular and participate in cell signaling. There are by transcytosis. More recently, they have intercellular communication. three classes of molecules: enzymes that been found to be sites where small mole- generate messengers from substrates in cules are concentrated and internalized by Caveolae the environment, high-affinity binding a process called potocytosis. A growing sites that concentrate chemical signals, body of biochemical and morphological Each caveola is a dynamic piece ofmem- and substrates that are enzymatically evidence indicates that a variety of mole- brane that is either open for receiving and converted into messengers. cules known to function directly or indi- releasing material or closed for process- GPI. Insulin was the first hormone rectly in signal transduction are enriched ing, storage, and delivery to the cell (11). suspected of using inositol phosphogly- in caveolae. This raises the possibility that The exact nature of the closed compart- can (IPG) or a molecule derived from IPG a third function for caveolae is to process ment is still unclear. -
Membrane Capacitance Recordings Resolve Dynamics and Complexity Of
www.nature.com/scientificreports OPEN Membrane capacitance recordings resolve dynamics and complexity of receptor-mediated endocytosis in Received: 22 October 2018 Accepted: 20 August 2019 Wnt signalling Published: xx xx xxxx Vera Bandmann1, Ann Schirin Mirsanaye1, Johanna Schäfer1, Gerhard Thiel1, Thomas Holstein2 & Melanie Mikosch-Wersching1,2 Receptor-mediated endocytosis is an essential process in signalling pathways for activation of intracellular signalling cascades. One example is the Wnt signalling pathway that seems to depend on endocytosis of the ligand-receptor complex for initiation of Wnt signal transduction. To date, the roles of diferent endocytic pathways in Wnt signalling, molecular players and the kinetics of the process remain unclear. Here, we monitored endocytosis in Wnt3a and Wnt5a-mediated signalling with membrane capacitance recordings of HEK293 cells. Our measurements revealed a swift and substantial increase in the number of endocytic vesicles. Extracellular Wnt ligands specifcally triggered endocytotic activity, which started immediately upon ligand binding and ceased within a period of ten minutes. By using specifc inhibitors, we were able to separate Wnt-induced endocytosis into two independent pathways. We demonstrate that canonical Wnt3a is taken up mainly by clathrin-independent endocytosis whereas noncanonical Wnt5a is exclusively regulated via clathrin-mediated endocytosis. Our fndings show that membrane capacitance recordings allow the resolution of complex cellular processes in plasma membrane signalling pathways in great detail. Wnt signalling is a highly-conserved signalling pathway with important functions in development, tissue-homeostasis, stem cell biology and many diseases, including cancer. Afer three decades of dedicated research we have come to understand many of the fundamental components of Wnt signalling pathways.