LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: Mul1 restrains Parkin-mediated mitophagy in mature neurons by maintaining ER-mitochondrial contacts

    Rajat Puri / Xiu-Tang Cheng / Mei-Yao Lin / Ning Huang / Zu-Hang Sheng

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 19

    Abstract: Little is known about the pathways that maintain mitochondrial structure and function under neuronal stress conditions. Here, authors demonstrate that the Mul1-Mfn2 pathway plays a checkpoint role in maintaining mitochondrial integrity and energy ... ...

    Abstract Little is known about the pathways that maintain mitochondrial structure and function under neuronal stress conditions. Here, authors demonstrate that the Mul1-Mfn2 pathway plays a checkpoint role in maintaining mitochondrial integrity and energy maintenance by ensuring ER-mitochondrial tethering and preventing mitophagy.
    Keywords Science ; Q
    Language English
    Publishing date 2019-08-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Mul1 restrains Parkin-mediated mitophagy in mature neurons by maintaining ER-mitochondrial contacts

    Rajat Puri / Xiu-Tang Cheng / Mei-Yao Lin / Ning Huang / Zu-Hang Sheng

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 19

    Abstract: Little is known about the pathways that maintain mitochondrial structure and function under neuronal stress conditions. Here, authors demonstrate that the Mul1-Mfn2 pathway plays a checkpoint role in maintaining mitochondrial integrity and energy ... ...

    Abstract Little is known about the pathways that maintain mitochondrial structure and function under neuronal stress conditions. Here, authors demonstrate that the Mul1-Mfn2 pathway plays a checkpoint role in maintaining mitochondrial integrity and energy maintenance by ensuring ER-mitochondrial tethering and preventing mitophagy.
    Keywords Science ; Q
    Language English
    Publishing date 2019-08-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Fibroblast activation protein (FAP) is essential for the migration of bone marrow mesenchymal stem cells through RhoA activation.

    Kuei-Min Chung / Shu-Ching Hsu / Yue-Ru Chu / Mei-Yao Lin / Weir-Tong Jiaang / Ruey-Hwa Chen / Xin Chen

    PLoS ONE, Vol 9, Iss 2, p e

    2014  Volume 88772

    Abstract: BACKGROUND: The ability of human bone marrow mesenchymal stem cells (BM-MSCs) to migrate and localize specifically to injured tissues is central in developing therapeutic strategies for tissue repair and regeneration. Fibroblast activation protein (FAP) ... ...

    Abstract BACKGROUND: The ability of human bone marrow mesenchymal stem cells (BM-MSCs) to migrate and localize specifically to injured tissues is central in developing therapeutic strategies for tissue repair and regeneration. Fibroblast activation protein (FAP) is a cell surface serine protease expressed at sites of tissue remodeling during embryonic development. It is also expressed in BM-MSCs, but not in normal tissues or cells. The function of FAP in BM-MSCs is not known. PRINCIPAL FINDINGS: We found that depletion of FAP proteins significantly inhibited the migration of BM-MSCs in a transwell chemotaxis assay. Such impaired migration ability of BM-MSCs could be rescued by re-expressing FAP in these cells. We then demonstrated that depletion of FAP activated intracellular RhoA GTPase. Consistently, inhibition of RhoA activity using a RhoA inhibitor rescued its migration ability. Inhibition of FAP activity with an FAP-specific inhibitor did not affect the activation of RhoA or the migration of BM-MSCs. Furthermore, the inflammatory cytokines interleukin-1beta (IL-1β) and transforming growth factor-beta (TGF-β) upregulated FAP expression, which coincided with better BM-MSC migration. CONCLUSIONS: Our results indicate FAP plays an important role in the migration of BM-MSCs through modulation of RhoA GTPase activity. The peptidase activity of FAP is not essential for such migration. Cytokines IL-1β and TGF-β upregulate the expression level of FAP and thus enhance BM-MSC migration.
    Keywords Medicine ; R ; Science ; Q
    Subject code 616
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article: Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination

    Liu, Chin-Chih / Chun-Ming Chen / Hsuan-An Chen / Liang-Yu Pang / Mei-Yao Lin / Pei-Rung Wu / Ruey-Hwa Chen / Si-Tse Jiang / Ting-Fen Tsai / Yu-Ching Lin / Yu-Hsuan Chen

    Molecular cell. 2016 Jan. 07, v. 61, no. 1

    2016  

    Abstract: Autophagy, a cellular self-eating mechanism, is important for maintaining cell survival and tissue homeostasis in various stressed conditions. Although the molecular mechanism of autophagy induction has been well studied, how cells terminate autophagy ... ...

    Abstract Autophagy, a cellular self-eating mechanism, is important for maintaining cell survival and tissue homeostasis in various stressed conditions. Although the molecular mechanism of autophagy induction has been well studied, how cells terminate autophagy process remains elusive. Here, we show that ULK1, a serine/threonine kinase critical for autophagy initiation, is a substrate of the Cul3-KLHL20 ubiquitin ligase. Upon autophagy induction, ULK1 autophosphorylation facilitates its recruitment to KLHL20 for ubiquitination and proteolysis. This autophagy-stimulated, KLHL20-dependent ULK1 degradation restrains the amplitude and duration of autophagy. Additionally, KLHL20 governs the degradation of ATG13, VPS34, Beclin-1, and ATG14 in prolonged starvation through a direct or indirect mechanism. Impairment of KLHL20-mediated regulation of autophagy dynamics potentiates starvation-induced cell death and aggravates diabetes-associated muscle atrophy. Our study identifies a key role of KLHL20 in autophagy termination by controlling autophagy-dependent turnover of ULK1 and VPS34 complex subunits and reveals the pathophysiological functions of this autophagy termination mechanism.
    Keywords autophagy ; cell viability ; homeostasis ; muscular atrophy ; protein phosphorylation ; protein-serine-threonine kinases ; proteolysis ; serine ; starvation ; threonine ; ubiquitination ; ubiquitin-protein ligase
    Language English
    Dates of publication 2016-0107
    Size p. 84-97.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2015.11.001
    Database NAL-Catalogue (AGRICOLA)

    Full text online

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article: K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

    Yuan, Wei-Chien / Cheng-Hsin Liu / Chin-Chun Hung / Jean-Cheng Kuo / Li-Ying Chang / Mei-Yao Lin / Ming Xu / Ruey-Hwa Chen / Shu-Yu Lin / Yen Pei Tan / Yu-Ru Lee / Zhijian J. Chen

    Molecular cell. 2014 May 22, v. 54

    2014  

    Abstract: Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the ... ...

    Abstract Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the Cullin 3 (Cul3) substrate adaptor KLHL20 is localized to the trans-Golgi network (TGN) and is important for post-Golgi trafficking by promoting the biogenesis of TGN-derived transport carriers. The Cul3-KLHL20 ubiquitin E3 ligase catalyzes a nondegradable, K33-linked polyubiquitination on coronin 7 (Crn7), which facilitates Crn7 targeting to TGN through a ubiquitin-dependent interaction with Eps15. Blockage of K33-chain formation, Crn7 ubiquitination, or disruption of Crn7-Eps15 interaction impairs TGN-pool F-actin assembly, a process essential for generating transport carriers. Enforced targeting of Crn7 to TGN bypasses the requirement of K33-ubiquitination for TGN-pool F-actin assembly and post-Golgi trafficking. Our study reveals a role of KLHL20-mediated K33-ubiquitination of Crn7 in post-Golgi transport and identifies a cellular recognition mechanism for this ubiquitin chain type.
    Keywords actin ; biogenesis ; polymers ; protein transport ; ubiquitin ; ubiquitination ; ubiquitin-protein ligase
    Language English
    Dates of publication 2014-0522
    Size p. 586-600.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2014.03.035
    Database NAL-Catalogue (AGRICOLA)

    Full text online

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top