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Traffic 8건

  1. [해외논문]   Issue Information  


    Traffic v.19 no.8 ,pp. 565 - 567 , 2018 , 1398-9219 ,

    초록

    원문보기

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    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  2. [해외논문]   Tying trafficking to fusion and fission at the mighty mitochondria   SCIE

    Farmer, Trey (The Department of Biochemistry and Molecular Biology, The University of Nebraska Medical Center, Omaha, Nebraska ) , Naslavsky, Naava (The Department of Biochemistry and Molecular Biology, The University of Nebraska Medical Center, Omaha, Nebraska ) , Caplan, Steve (The Department of Biochemistry and Molecular Biology, The University of Nebraska Medical Center, Omaha, Nebraska)
    Traffic v.19 no.8 ,pp. 569 - 577 , 2018 , 1398-9219 ,

    초록

    The mitochondrion is a unique organelle that serves as the main site of ATP generation needed for energy in the cell. However, mitochondria also play essential roles in cell death through apoptosis and necrosis, as well as a variety of crucial functions related to stress regulation, autophagy, lipid synthesis and calcium storage. There is a growing appreciation that mitochondrial function is regulated by the dynamics of its membrane fusion and fission; longer, fused mitochondria are optimal for ATP generation, whereas fission of mitochondria facilitates mitophagy and cell division. Despite the significance of mitochondrial homeostasis for such crucial cellular events, the intricate regulation of mitochondrial fusion and fission is only partially understood. Until very recently, only a single mitochondrial fission protein had been identified. Moreover, only now have researchers turned to address the upstream machinery that regulates mitochondrial fusion and fission proteins. Herein, we review the known GTPases involved in mitochondrial fusion and fission, but also highlight recent studies that address the mechanisms by which these GTPases are regulated. In particular, we draw attention to a substantial new body of literature linking endocytic regulatory proteins, such as the retromer VPS35 cargo selection complex subunit, to mitochondrial homeostasis. These recent studies suggest that relationships and cross‐regulation between endocytic and mitochondrial pathways may be more widespread than previously assumed.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  3. [해외논문]   Endosomal receptor trafficking: Retromer and beyond   SCIE

    Wang, Jing (Key Laboratory of Birth Defects and Related Diseases of Women and Children, Department of Pediatrics, Division of Neurology, West China Second University Hospital, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, Sichuan University, Chengdu, China) , Fedoseienko, Alina (Division of Oncology Research, Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota ) , Chen, Baoyu (Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, Iowa ) , Burstein, Ezra (Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas ) , Jia, Da (Key Laboratory of Birth Defects and Related Diseases of Women and Children, Department of Pediatrics, Division of Neurology, West China Second University Hospital, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, Sichuan University, Chengdu, China) , Billadeau, Daniel D. (Division of Oncology Re)
    Traffic v.19 no.8 ,pp. 578 - 590 , 2018 , 1398-9219 ,

    초록

    The tubular endolysosomal network is a quality control system that ensures the proper delivery of internalized receptors to specific subcellular destinations in order to maintain cellular homeostasis. Although retromer was originally described in yeast as a regulator of endosome‐to‐Golgi receptor recycling, mammalian retromer has emerged as a central player in endosome‐to‐plasma membrane recycling of a variety of receptors. Over the past decade, information regarding the mechanism by which retromer facilitates receptor trafficking has emerged, as has the identification of numerous retromer‐associated molecules including the WASH complex, sorting nexins (SNXs) and TBC1d5. Moreover, the recent demonstration that several SNXs can directly interact with retromer cargo to facilitate endosome‐to‐Golgi retrieval has provided new insight into how these receptors are trafficked in cells. The mechanism by which SNX17 cargoes are recycled out of the endosomal system was demonstrated to involve a retromer‐like complex termed the retriever, which is recruited to WASH positive endosomes through an interaction with the COMMD/CCDC22/CCDC93 (CCC) complex. Lastly, the mechanisms by which bacterial and viral pathogens highjack this complex sorting machinery in order to escape the endolysosomal system or remain hidden within the cells are beginning to emerge. In this review, we will highlight recent studies that have begun to unravel the intricacies by which the retromer and associated molecules contribute to receptor trafficking and how deregulation at this sorting domain can contribute to disease or facilitate pathogen infection.

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    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  4. [해외논문]   7‐Ketocholesterol impairs phagocytosis and efferocytosis via dysregulation of phosphatidylinositol 4,5‐bisphosphate   SCIE

    Lu, Stella M. (Department of Biochemistry, University of Toronto, Toronto, ON, Canada) , Fairn, Gregory D. (Department of Biochemistry, University of Toronto, Toronto, ON, Canada)
    Traffic v.19 no.8 ,pp. 591 - 604 , 2018 , 1398-9219 ,

    초록

    The plasma membrane is inhomogeneously organized containing both highly ordered and disordered nanodomains. 7‐Ketocholesterol (7KC), an oxysterol formed from the nonenzymatic oxidation of cholesterol, is a potent disruptor of membrane order. Importantly, 7KC is a component of oxidized low‐density lipoprotein and accumulates in macrophage and foam cells found in arterial plaques. Using a murine macrophage cell line, J774, we report that both IgG‐mediated and phosphatidylserine‐mediated phagocytic pathways are inhibited by the accumulation of 7KC. Examination of the well‐studied Fcγ receptor pathway revealed that the cell surface receptor abundance and ligand binding are unaltered while downstream signaling and activation of spleen tyrosine kinase is not affected. However, while the recruitment of phospholipase Cγ1 was unaffected its apparent enzymatic activity was compromised resulting in sustained phosphatidylinositol 4,5‐bisphosphate [PtdIns(4,5)P 2 ] levels and polymerized actin at the base of the phagocytic cup. Additionally, we found that 7KC prevented the activation of PLCβ downstream of the P2Y 6 G‐protein coupled receptor and that 7KC impaired PLCγ activity in response to a direct elevation of cytosolic calcium induced by ionomycin. Finally, we demonstrate that 7KC partly attenuates the activity of rapamycin recruitable constitutively active PLCβ3. Together, our results demonstrate that the accumulation of 7KC impairs macrophage function by altering PtdIns(4,5)P 2 catabolism and, thus, impairing actin depolymerization required for the completion of phagocytosis.

    원문보기

    원문보기
    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

    Fig. 1 이미지
  5. [해외논문]   Spatial organization of protein export in malaria parasite blood stages   SCIE

    Charnaud, Sarah C. (Burnet Institute, Melbourne, Australia) , Jonsdottir, Thorey K. (Burnet Institute, Melbourne, Australia) , Sanders, Paul R. (Burnet Institute, Melbourne, Australia) , Bullen, Hayley E. (Burnet Institute, Melbourne, Australia) , Dickerman, Benjamin K. (Burnet Institute, Melbourne, Australia) , Kouskousis, Betty (Burnet Institute, Melbourne, Australia) , Palmer, Catherine S. (Burnet Institute, Melbourne, Australia) , Pietrzak, Halina M. (Burnet Institute, Melbourne, Australia) , Laumaea, Annamarie E. (Burnet Institute, Melbourne, Australia) , Erazo, Anna‐ (Burnet Institute, Melbourne, Australia) , Belen (Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Australia) , McHugh, Emma (Department of Biochemistry and Molecular Biology, University of Melbourne,) , Tilley, Leann , Crabb, Brendan S. , Gilson, Paul R.
    Traffic v.19 no.8 ,pp. 605 - 623 , 2018 , 1398-9219 ,

    초록

    Plasmodium falciparum , which causes malaria, extensively remodels its human host cells, particularly erythrocytes. Remodelling is essential for parasite survival by helping to avoid host immunity and assisting in the uptake of plasma nutrients to fuel rapid growth. Host cell renovation is carried out by hundreds of parasite effector proteins that are exported into the erythrocyte across an enveloping parasitophorous vacuole membrane (PVM). The Plasmodium translocon for exported (PTEX) proteins is thought to span the PVM and provide a channel that unfolds and extrudes proteins across the PVM into the erythrocyte. We show that exported reporter proteins containing mouse dihydrofolate reductase domains that inducibly resist unfolding become trapped at the parasite surface partly colocalizing with PTEX. When cargo is trapped, loop‐like extensions appear at the PVM containing both trapped cargo and PTEX protein EXP2, but not additional components HSP101 and PTEX150. Following removal of the block‐inducing compound, export of reporter proteins only partly recovers possibly because much of the trapped cargo is spatially segregated in the loop regions away from PTEX. This suggests that parasites have the means to isolate unfoldable cargo proteins from PTEX‐containing export zones to avert disruption of protein export that would reduce parasite growth.

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    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

    Fig. 1 이미지
  6. [해외논문]   Vacuole membrane protein 1 marks endoplasmic reticulum subdomains enriched in phospholipid synthesizing enzymes and is required for phosphoinositide distribution   SCIE

    Tá (Instituto de Investigaciones Biomédicas Alberto Sols, C.S.I.C./U.A.M., Madrid, Spain) , bara, Luis‐ (Department of Physiology and Biophysics, School of Medicine, University of Washington, Seattle, Washington ) , Carlos (Department of Biosciences, University of Helsinki, Helsinki, Finland) , Vicente, Juan‐ (Department of Biosciences, University of Helsinki, Helsinki, Finland) , Jesú (Instituto de Investigaciones Biomédicas Alberto Sols, C.S.I.C./U.A.M., Madrid, Spain) , s (Instituto de Investigaciones Biomédicas Alberto Sols, C.S.I.C./U.A.M., Madrid, Spain) , Biazik, Joanna , Eskelinen, Eeva‐ , Liisa , Vincent, Olivier , Escalante, Ricardo
    Traffic v.19 no.8 ,pp. 624 - 638 , 2018 , 1398-9219 ,

    초록

    The multispanning membrane protein vacuole membrane protein 1 (VMP1) marks and regulates endoplasmic reticulum (ER)‐domains associated with diverse ER‐organelle membrane contact sites. A proportion of these domains associate with endosomes during their maturation and remodeling. We found that these VMP1 domains are enriched in choline/ethanolamine phosphotransferase and phosphatidylinositol synthase (PIS1), 2 ER enzymes required for the synthesis of various phospholipids. Interestingly, the lack of VMP1 impairs the formation of PIS1‐enriched ER domains, suggesting a role in the distribution of phosphoinositides. In fact, depletion of VMP1 alters the distribution of PtdIns4P and proteins involved in the trafficking of PtdIns4P. Consistently, in these conditions, defects were observed in endosome trafficking and maturation as well as in Golgi morphology. We propose that VMP1 regulates the formation of ER domains enriched in lipid synthesizing enzymes. These domains might be necessary for efficient distribution of PtdIns4P and perhaps other lipid species. These findings, along with previous reports that involved VMP1 in regulating PtdIns3P during autophagy, expand the role of VMP1 in lipid trafficking and explain the pleiotropic effects observed in VMP1‐deficient mammalian cells and other model systems.

    원문보기

    원문보기
    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

    Fig. 1 이미지
  7. [해외논문]   Combining high‐pressure freezing with pre‐embedding immunogold electron microscopy and tomography   SCIE

    Hess, Michael W. (Division of Histology and Embryology, Medical University of Innsbruck, Innsbruck, Austria) , Vogel, Georg F. (Division of Histology and Embryology, Medical University of Innsbruck, Innsbruck, Austria) , Yordanov, Teodor E. (Division of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria) , Witting, Barbara (Division of Histology and Embryology, Medical University of Innsbruck, Innsbruck, Austria) , Gutleben, Karin (Division of Histology and Embryology, Medical University of Innsbruck, Innsbruck, Austria) , Ebner, Hannes L. (Division of Histology and Embryology, Medical University of Innsbruck, Innsbruck, Austria) , de Araujo, Mariana E. G. (Division of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria) , Filipek, Przemyslaw A. (Division of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria<cou) , Huber, Lukas A.
    Traffic v.19 no.8 ,pp. 639 - 649 , 2018 , 1398-9219 ,

    초록

    Immunogold labeling of permeabilized whole‐mount cells or thin‐sectioned material is widely used for the subcellular localization of biomolecules at the high spatial resolution of electron microscopy (EM). Those approaches are well compatible with either 3‐dimensional (3D) reconstruction of organelle morphology and antigen distribution or with rapid cryofixation—but not easily with both at once. We describe here a specimen preparation and labeling protocol for animal cell cultures, which represents a novel blend of specifically adapted versions of established techniques. It combines the virtues of reliably preserved organelle ultrastructure, as trapped by rapid freezing within milliseconds followed by freeze‐substitution and specimen rehydration, with the advantages of robust labeling of intracellular constituents in 3D through means of pre‐embedding NANOGOLD‐silver immunocytochemistry. So obtained thin and semi‐thick epoxy resin sections are suitable for transmission EM imaging, as well as tomographic reconstruction and modeling of labeling patterns in the 3D cellular context.

    원문보기

    원문보기
    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

    Fig. 1 이미지
  8. [해외논문]   Correction to: Nup42 and IP6 coordinate Gle1 stimulation of Dbp5/DDX19B for mRNA export in yeast and human cells  

    Adams, Rebecca L. (Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee ) , Mason, Aaron C. (Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee ) , Glass, Laura (Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee ) , Aditi, (Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee) , Wente, Susan R.
    Traffic v.19 no.8 ,pp. 650 - 650 , 2018 , 1398-9219 ,

    초록

    Immunogold labeling of permeabilized whole‐mount cells or thin‐sectioned material is widely used for the subcellular localization of biomolecules at the high spatial resolution of electron microscopy (EM). Those approaches are well compatible with either 3‐dimensional (3D) reconstruction of organelle morphology and antigen distribution or with rapid cryofixation—but not easily with both at once. We describe here a specimen preparation and labeling protocol for animal cell cultures, which represents a novel blend of specifically adapted versions of established techniques. It combines the virtues of reliably preserved organelle ultrastructure, as trapped by rapid freezing within milliseconds followed by freeze‐substitution and specimen rehydration, with the advantages of robust labeling of intracellular constituents in 3D through means of pre‐embedding NANOGOLD‐silver immunocytochemistry. So obtained thin and semi‐thick epoxy resin sections are suitable for transmission EM imaging, as well as tomographic reconstruction and modeling of labeling patterns in the 3D cellular context.

    원문보기

    원문보기
    무료다운로드 유료다운로드

    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

    이미지

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