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  1. Article ; Online: A tango for coats and membranes: New insights into ER-to-Golgi traffic.

    Aridor, Meir

    Cell reports

    2022  Volume 38, Issue 3, Page(s) 110258

    Abstract: The realization that the meticulous organization of cellular organelles is not required for the reconstitution of select intracellular traffic steps has revolutionized cell biology. It transformed the discipline from a morphological one into a molecular ... ...

    Abstract The realization that the meticulous organization of cellular organelles is not required for the reconstitution of select intracellular traffic steps has revolutionized cell biology. It transformed the discipline from a morphological one into a molecular one. It helped in defining the activities of COPII and COPI vesicle coats in secretion. The work established the principles of the vesicular traffic model as envisioned by George Palade 50 years ago. However, in recent years, numerous advances in cellular and imaging technologies afforded an unprecedented molecular resolution that sheds new light on COPII activities and biosynthetic traffic between the ER and the Golgi. In the following review, I summarize this new information and attempt to provide a unified physical-molecular-morphological description of this traffic step. This information expands on the simplistic principles of vesicular traffic and provides novel frameworks to examine and explain physiological secretion.
    MeSH term(s) Animals ; COP-Coated Vesicles/metabolism ; Coat Protein Complex I/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Humans ; Protein Transport/physiology
    Chemical Substances Coat Protein Complex I
    Language English
    Publishing date 2022-01-19
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2021.110258
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  2. Article ; Online: COPII gets in shape: Lessons derived from morphological aspects of early secretion.

    Aridor, Meir

    Traffic (Copenhagen, Denmark)

    2018  Volume 19, Issue 11, Page(s) 823–839

    Abstract: Our view of the secretory pathway has evolved from a morphological one to one that includes molecular mechanistic understanding of basic traffic components. These components include coat complexes involved in cargo sorting and budding and proteins that ... ...

    Abstract Our view of the secretory pathway has evolved from a morphological one to one that includes molecular mechanistic understanding of basic traffic components. These components include coat complexes involved in cargo sorting and budding and proteins that mediate targeting, tethering and fusion. The expanding repertoire of regulators that control basic traffic activities begins to paint a unified morphological-molecular view of secretion. The emerging picture provides key insights into the coupling of secretion with physiology. This review examines aspects of morphological-molecular relations that are derived from studies on traffic from the endoplasmic reticulum carried by the coat protein complex II.
    MeSH term(s) Animals ; COP-Coated Vesicles/metabolism ; Humans ; Protein Transport ; Secretory Pathway
    Language English
    Publishing date 2018-08-02
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12603
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  3. Article ; Online: Linton Mark Traub (1962-2020).

    Aridor, Meir / Owen, David J

    The Journal of cell biology

    2021  Volume 220, Issue 2

    Language English
    Publishing date 2021-01-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202011169
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  4. Article: Living the DReaM: The interrelations between statistical, scientific and nature of science uncertainty articulations through citizen science.

    Aridor, Keren / Dvir, Michal / Tsybulsky, Dina / Ben-Zvi, Dani

    Instructional science

    2023  , Page(s) 1–34

    Abstract: Responsible citizenship and sound decision-making in today's information age necessitate an appreciation of the role of uncertainty in the process of generating data-based scientific knowledge. The latter calls for coordinating between different types of ...

    Abstract Responsible citizenship and sound decision-making in today's information age necessitate an appreciation of the role of uncertainty in the process of generating data-based scientific knowledge. The latter calls for coordinating between different types of uncertainties, related to three types of relevant reasoning: statistical, scientific, and nature of science uncertainties. This article examines separately the uncertainties that young students articulate as they engage in activities designed to concurrently foster all three types of reasoning, and also explores how these different types can interrelate. The context of Citizen Science is particularly suited for this goal, providing a unique pedagogical opportunity for learning scientific content by engaging learners in authentic scientific practices, including data analysis. Based on literature from the three fields of statistics, science and nature of science education, we offer an integrative framework, Deterministic Relativistic and Middle ground (DReaM), which consists of nine sub-categories of uncertainty articulations. We utilize it to analyze an instrumental case study of a pair of middle school students' (ages 13 and 14) participation in a pilot study of an interdisciplinary extended learning sequence, as part of the Radon Citizen Science Project. The results of an interpretative microgenetic analysis identified all nine DReaM uncertainty articulations sub-categories. These are illustrated in the Findings section with key scenes from the pair's participation. The discussion depicts how these sub-categories manifested in this particular case study and suggests interrelations between them in a more extended depiction of the DReaM framework. We conclude with the pedagogical implications of the extended framework.
    Language English
    Publishing date 2023-04-19
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2015666-2
    ISSN 1573-1952 ; 0020-4277
    ISSN (online) 1573-1952
    ISSN 0020-4277
    DOI 10.1007/s11251-023-09626-8
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  5. Article: Visiting the ER: the endoplasmic reticulum as a target for therapeutics in traffic related diseases.

    Aridor, Meir

    Advanced drug delivery reviews

    2007  Volume 59, Issue 8, Page(s) 759–781

    Abstract: The endoplasmic reticulum (ER) is a central processor that controls the expression of functional proteins, required for the communication of the cell with the external environment. Plasma membranes receptors, ion channels, secreted hormones, catabolic ... ...

    Abstract The endoplasmic reticulum (ER) is a central processor that controls the expression of functional proteins, required for the communication of the cell with the external environment. Plasma membranes receptors, ion channels, secreted hormones, catabolic and metabolic enzymes are folded and assembled in the ER. Key metabolic functions are also regulated from the ER. Molecular quality control monitors ER processing activities and co-ordinates these activities with cell and organism demands. Recent understandings of the molecular basis for ER processing activities illuminate the key role of the ER in the development of a variety of diseases. ER derived diseases include specific genetic disorders such as cystic fibrosis or highly prevalent diseases including diabetes and a range of neurodegenerative diseases. ER processing also plays a key role in the development of cancer. This review summarizes the molecular basis for ER processing functions and current avenues in ER-targeted drug development.
    MeSH term(s) Animals ; Apoptosis/drug effects ; Biological Transport/drug effects ; COP-Coated Vesicles/drug effects ; COP-Coated Vesicles/metabolism ; Diabetes Mellitus/drug therapy ; Diabetes Mellitus/metabolism ; Drug Delivery Systems ; Endoplasmic Reticulum/metabolism ; Glycosylation/drug effects ; Hypoxia/drug therapy ; Hypoxia/metabolism ; Molecular Chaperones/administration & dosage ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/metabolism ; Neuroprotective Agents/chemistry ; Neuroprotective Agents/pharmacology ; Protein Biosynthesis/drug effects ; Protein Conformation/drug effects ; Protein Folding ; Protein Processing, Post-Translational/drug effects ; Protein Transport/drug effects ; Transport Vesicles/drug effects
    Chemical Substances Molecular Chaperones ; Neuroprotective Agents
    Language English
    Publishing date 2007-08-10
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 639113-8
    ISSN 1872-8294 ; 0169-409X
    ISSN (online) 1872-8294
    ISSN 0169-409X
    DOI 10.1016/j.addr.2007.06.002
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  6. Article ; Online: Selective targeting of ER exit sites supports axon development.

    Aridor, Meir / Fish, Kenneth N

    Traffic (Copenhagen, Denmark)

    2009  Volume 10, Issue 11, Page(s) 1669–1684

    Abstract: During neuron development, the biosynthetic needs of the axon initially outweigh those of dendrites. However, although a localized role for the early secretory pathway in dendrite development has been observed, such a role in axon growth remains ... ...

    Abstract During neuron development, the biosynthetic needs of the axon initially outweigh those of dendrites. However, although a localized role for the early secretory pathway in dendrite development has been observed, such a role in axon growth remains undefined. We therefore studied the localization of Sar1, a small GTPase that controls ER export, during early stages of neuronal development that are characterized by selective and robust axon growth. At these early stages, Sar1 was selectively targeted to the axon where it gradually concentrated within varicosities in which additional proteins that function in the early secretory pathway were detected. Sar1 targeting to the axon followed axon specification and was dependent on localized actin instability. Changes in Sar1 expression levels at these early development stages modulated axon growth. Specifically, reduced expression of Sar1, which was initially only detectable in the axon, correlated with reduced axon growth, where as overexpression of Sar1 supported the growth of longer axons. In support of the former finding, expression of dominant negative Sar1 inhibited axon growth. Thus, as observed in lower organisms, mammalian cells use temporal and spatial regulation of endoplasmic reticulum exit site (ERES) to address developmental biosynthetic demands. Furthermore, axons, such as dendrites, rely on ERES targeting and assembly for growth.
    MeSH term(s) Animals ; Axons/metabolism ; COP-Coated Vesicles/metabolism ; Cells, Cultured ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Hippocampus/cytology ; Mice ; Mice, Knockout ; Monomeric GTP-Binding Proteins/genetics ; Monomeric GTP-Binding Proteins/metabolism ; Neurons/metabolism ; Protein Binding ; Rats ; Rats, Sprague-Dawley
    Chemical Substances SAR1 protein, rat (EC 3.6.1.-) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2009-08-05
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/j.1600-0854.2009.00974.x
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  7. Article: Selective Targeting of ER Exit Sites Supports Axon Development

    Aridor, Meir / Fish, Kenneth N

    Traffic. 2009 Nov., v. 10, no. 11

    2009  

    Abstract: During neuron development, the biosynthetic needs of the axon initially outweigh those of dendrites. However, although a localized role for the early secretory pathway in dendrite development has been observed, such a role in axon growth remains ... ...

    Abstract During neuron development, the biosynthetic needs of the axon initially outweigh those of dendrites. However, although a localized role for the early secretory pathway in dendrite development has been observed, such a role in axon growth remains undefined. We therefore studied the localization of Sar1, a small GTPase that controls ER export, during early stages of neuronal development that are characterized by selective and robust axon growth. At these early stages, Sar1 was selectively targeted to the axon where it gradually concentrated within varicosities in which additional proteins that function in the early secretory pathway were detected. Sar1 targeting to the axon followed axon specification and was dependent on localized actin instability. Changes in Sar1 expression levels at these early development stages modulated axon growth. Specifically, reduced expression of Sar1, which was initially only detectable in the axon, correlated with reduced axon growth, where as overexpression of Sar1 supported the growth of longer axons. In support of the former finding, expression of dominant negative Sar1 inhibited axon growth. Thus, as observed in lower organisms, mammalian cells use temporal and spatial regulation of endoplasmic reticulum exit site (ERES) to address developmental biosynthetic demands. Furthermore, axons, such as dendrites, rely on ERES targeting and assembly for growth.
    Keywords endoplasmic reticulum
    Language English
    Dates of publication 2009-11
    Size p. 1669-1684.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/j.1600-0854.2009.00974.x
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  8. Article ; Online: VAMP-associated Proteins (VAP) as Receptors That Couple Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Proteostasis with Lipid Homeostasis.

    Ernst, Wayne L / Shome, Kuntala / Wu, Christine C / Gong, Xiaoyan / Frizzell, Raymond A / Aridor, Meir

    The Journal of biological chemistry

    2016  Volume 291, Issue 10, Page(s) 5206–5220

    Abstract: Unesterified cholesterol accumulates in late endosomes in cells expressing the misfolded cystic fibrosis transmembrane conductance regulator (CFTR). CFTR misfolding in the endoplasmic reticulum (ER) or general activation of ER stress led to dynein- ... ...

    Abstract Unesterified cholesterol accumulates in late endosomes in cells expressing the misfolded cystic fibrosis transmembrane conductance regulator (CFTR). CFTR misfolding in the endoplasmic reticulum (ER) or general activation of ER stress led to dynein-mediated clustering of cholesterol-loaded late endosomes at the Golgi region, a process regulated by ER-localized VAMP-associated proteins (VAPs). We hypothesized that VAPs serve as intracellular receptors that couple lipid homeostasis through interactions with two phenylalanines in an acidic track (FFAT) binding signals (found in lipid sorting and sensing proteins, LSS) with proteostasis regulation. VAPB inhibited the degradation of ΔF508-CFTR. The activity was mapped to the ligand-binding major sperm protein (MSP) domain, which was sufficient in regulating CFTR biogenesis. We identified mutations in an unstructured loop within the MSP that uncoupled VAPB-regulated CFTR biogenesis from basic interactions with FFAT. Using this information, we defined functional and physical interactions between VAPB and proteostasis regulators (ligands), including the unfolded protein response sensor ATF6 and the ER degradation cluster that included FAF1, VCP, BAP31, and Derlin-1. VAPB inhibited the degradation of ΔF508-CFTR in the ER through interactions with the RMA1-Derlin-BAP31-VCP pathway. Analysis of pseudoligands containing tandem FFAT signals supports a competitive model for VAP interactions that direct CFTR biogenesis. The results suggest a model in which VAP-ligand binding couples proteostasis and lipid homeostasis leading to observed phenotypes of lipid abnormalities in protein folding diseases.
    MeSH term(s) Adaptor Proteins, Signal Transducing ; Adenosine Triphosphatases ; Apoptosis Regulatory Proteins ; Binding Sites ; Cell Cycle Proteins ; Cholesterol/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism ; DNA-Binding Proteins/metabolism ; HEK293 Cells ; HeLa Cells ; Homeostasis ; Humans ; Membrane Proteins/metabolism ; Protein Binding ; Protein Stability ; Proteolysis ; Ubiquitin-Protein Ligases/metabolism ; Valosin Containing Protein ; Vesicular Transport Proteins/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; BCAP31 protein, human ; Cell Cycle Proteins ; DERL1 protein, human ; DNA-Binding Proteins ; FAF1 protein, human ; Membrane Proteins ; VAPB protein, human ; Vesicular Transport Proteins ; cystic fibrosis transmembrane conductance regulator delta F508 ; Cystic Fibrosis Transmembrane Conductance Regulator (126880-72-6) ; Cholesterol (97C5T2UQ7J) ; RNF5 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Adenosine Triphosphatases (EC 3.6.1.-) ; VCP protein, human (EC 3.6.4.6) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2016-01-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M115.692749
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  9. Article ; Online: A cascade of ER exit site assembly that is regulated by p125A and lipid signals.

    Klinkenberg, David / Long, Kimberly R / Shome, Kuntala / Watkins, Simon C / Aridor, Meir

    Journal of cell science

    2014  Volume 127, Issue Pt 8, Page(s) 1765–1778

    Abstract: The inner and outer layers of COPII mediate cargo sorting and vesicle biogenesis. Sec16A and p125A (officially known as SEC23IP) proteins interact with both layers to control coat activity, yet the steps directing functional assembly at ER exit sites ( ... ...

    Abstract The inner and outer layers of COPII mediate cargo sorting and vesicle biogenesis. Sec16A and p125A (officially known as SEC23IP) proteins interact with both layers to control coat activity, yet the steps directing functional assembly at ER exit sites (ERES) remain undefined. By using temperature blocks, we find that Sec16A is spatially segregated from p125A-COPII-coated ERES prior to ER exit at a step that required p125A. p125A used lipid signals to control ERES assembly. Within p125A, we defined a C-terminal DDHD domain found in phospholipases and PI transfer proteins that recognized PA and phosphatidylinositol phosphates in vitro and was targeted to PI4P-rich membranes in cells. A conserved central SAM domain promoted self-assembly and selective lipid recognition by the DDHD domain. A basic cluster and a hydrophobic interface in the DDHD and SAM domains, respectively, were required for p125A-mediated functional ERES assembly. Lipid recognition by the SAM-DDHD module was used to stabilize membrane association and regulate the spatial segregation of COPII from Sec16A, nucleating the coat at ERES for ER exit.
    MeSH term(s) Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; HeLa Cells ; Humans ; Hydrophobic and Hydrophilic Interactions ; Liposomes/metabolism ; Monomeric GTP-Binding Proteins/metabolism ; Phosphatidylinositol Phosphates/physiology ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Protein Transport ; RNA-Binding Proteins ; Vesicular Transport Proteins/metabolism
    Chemical Substances Carrier Proteins ; Liposomes ; Phosphatidylinositol Phosphates ; RNA-Binding Proteins ; SEC13 protein, human ; SEC16A protein, human ; SEC23A protein, human ; SEC23IP protein, human ; SEC24A protein, human ; SEC31A protein, human ; Vesicular Transport Proteins ; phosphatidylinositol 4-phosphate ; SAR1A protein, human (EC 3.6.1.-) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2014-02-12
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.138784
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  10. Article: Cargo selection in vesicular transport: the making and breaking of a coat.

    Aridor, Meir / Traub, Linton M

    Traffic (Copenhagen, Denmark)

    2002  Volume 3, Issue 8, Page(s) 537–546

    Abstract: Intracellular traffic is mediated by vesicular/tubular carriers. The carriers are formed by the activity of cytosolic coat proteins that are recruited to their target membranes and deform these membranes into buds and vesicles. Specific interactions ... ...

    Abstract Intracellular traffic is mediated by vesicular/tubular carriers. The carriers are formed by the activity of cytosolic coat proteins that are recruited to their target membranes and deform these membranes into buds and vesicles. Specific interactions between recruited coat subunits and short peptide sequences (transport motifs) on cargo proteins direct the incorporation of cargo into budded vesicles. Here, we focus on cargo selection reactions mediated by COPII and AP-2/clathrin vesicle coat complexes to explore common mechanisms by which coat assembly support localized and selective cargo sorting. Recent findings suggest that multiple, low-affinity interactions are employed in a cooperative manner to support coat assembly and enable cargo recognition. Thus low-binding affinities between coat subunits and transport motifs are transiently transformed into high-avidity, multivalent and selective interactions at vesicle bud sites. The temporal and regulated nature of the interactions provide the key to cargo selection.
    MeSH term(s) Animals ; COP-Coated Vesicles/metabolism ; Clathrin/metabolism ; Clathrin-Coated Vesicles/metabolism ; Coat Protein Complex I/metabolism ; Endocytosis ; Endoplasmic Reticulum/metabolism ; Humans ; Ligands ; Models, Biological ; Phosphatidylinositols/metabolism ; Protein Transport
    Chemical Substances Clathrin ; Coat Protein Complex I ; Ligands ; Phosphatidylinositols
    Language English
    Publishing date 2002-07-15
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1034/j.1600-0854.2002.30804.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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