LIVIVO - Search results -

Search results

Result 1 - 10 of total 23

Search options

Article ; Online: Allosteric regulation of noncoding RNA function by microRNAs.

Gorbea, Carlos / Elhakiem, Abdalla / Cazalla, Demián

2022 Volume 50, Issue 11, Page(s) 6511–6520

Abstract: HSUR1 and HSUR2, two noncoding RNAs expressed by the oncogenic Herpesvirus saimiri, bind host microRNAs miR-142-3p, miR-16, and miR-27 with different purposes. While binding of miR-27 to HSUR1 triggers the degradation of the microRNA, miR-16 is tethered ... ...

Abstract	HSUR1 and HSUR2, two noncoding RNAs expressed by the oncogenic Herpesvirus saimiri, bind host microRNAs miR-142-3p, miR-16, and miR-27 with different purposes. While binding of miR-27 to HSUR1 triggers the degradation of the microRNA, miR-16 is tethered by HSUR2 to target host mRNAs to repress their expression. Here we show that the interaction with miR-142-3p is required for the activity of both HSURs. Coimmunoprecipitation experiments revealed that miR-142-3p allosterically regulates the binding of miR-27 and miR-16 to HSUR1 and HSUR2, respectively. The binding of two different miRNAs to each HSUR is not cooperative. HSURs can be engineered to be regulated by other miRNAs, indicating that the identity of the binding miRNA is not important for HSUR regulation. Our results uncover a mechanism for allosteric regulation of noncoding RNA function and a previously unappreciated way in which microRNAs can regulate gene expression.
MeSH term(s)	Allosteric Regulation ; Herpesviridae Infections/metabolism ; Herpesvirus 2, Saimiriine/genetics ; MicroRNAs/genetics ; MicroRNAs/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Untranslated/genetics ; RNA, Untranslated/metabolism
Chemical Substances	MicroRNAs ; RNA, Messenger ; RNA, Untranslated
Language	English
Publishing date	2022-06-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkac443
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1067: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Shaping the host cell environment with viral noncoding RNAs.

Gorbea, Carlos / Elhakiem, Abdalla / Cazalla, Demián

Seminars in cell & developmental biology

2022 Volume 146, Page(s) 20–30

Abstract: Just like the cells they infect viruses express different classes of noncoding RNAs (ncRNAs). Viral ncRNAs come in all shapes and forms, and they usually associate with cellular proteins that are important for their functions. Viral ncRNAs have diverse ... ...

Abstract	Just like the cells they infect viruses express different classes of noncoding RNAs (ncRNAs). Viral ncRNAs come in all shapes and forms, and they usually associate with cellular proteins that are important for their functions. Viral ncRNAs have diverse functions, but they all contribute to the viral control of the cellular environment. Viruses utilize ncRNAs to regulate viral replication, to decide whether they should remain latent or reactivate, to evade the host immune responses, or to promote cellular transformation. In this review we describe the diverse functions played by different classes of ncRNAs expressed by adenoviruses and herpesviruses, how they contribute to the viral infection, and how their study led to insights into RNA-based mechanisms at play in host cells.
MeSH term(s)	Humans ; RNA, Viral/genetics ; RNA, Viral/metabolism ; RNA, Untranslated/genetics ; RNA, Untranslated/metabolism ; Viruses/genetics ; Viruses/metabolism ; Virus Diseases/genetics ; MicroRNAs ; RNA, Long Noncoding
Chemical Substances	RNA, Viral ; RNA, Untranslated ; MicroRNAs ; RNA, Long Noncoding
Language	English
Publishing date	2022-12-28
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2022.12.008
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2918: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Viral miRNA adaptor differentially recruits miRNAs to target mRNAs through alternative base-pairing.

Gorbea, Carlos / Mosbruger, Tim / Nix, David A / Cazalla, Demián

eLife

2019 Volume 8

Abstract: HSUR2 is a viral non-coding RNA (ncRNA) that functions as a microRNA (miRNA) adaptor. HSUR2 inhibits apoptosis in infected cells by recruiting host miRNAs miR-142-3p and miR-16 to mRNAs encoding apoptotic factors. HSUR2's target recognition mechanism is ... ...

Abstract	HSUR2 is a viral non-coding RNA (ncRNA) that functions as a microRNA (miRNA) adaptor. HSUR2 inhibits apoptosis in infected cells by recruiting host miRNAs miR-142-3p and miR-16 to mRNAs encoding apoptotic factors. HSUR2's target recognition mechanism is not understood. It is also unknown why HSUR2 utilizes miR-16 to downregulate only a subset of transcripts. We developed a general method for
MeSH term(s)	Animals ; Base Pairing ; Cell Line ; DNA Mutational Analysis ; Herpesvirus 2, Saimiriine/genetics ; Herpesvirus 2, Saimiriine/growth & development ; Host-Pathogen Interactions ; Humans ; MicroRNAs/genetics ; MicroRNAs/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Viral/genetics ; RNA, Viral/metabolism
Chemical Substances	MicroRNAs ; RNA, Messenger ; RNA, Viral
Language	English
Publishing date	2019-09-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.50530
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A viral Sm-class RNA base-pairs with mRNAs and recruits microRNAs to inhibit apoptosis.

Gorbea, Carlos / Mosbruger, Tim / Cazalla, Demián

Nature

2017 Volume 550, Issue 7675, Page(s) 275–279

Abstract: Viruses express several classes of non-coding RNAs; the functions and mechanisms by which most of these act are unknown. Herpesvirus saimiri, a γ-herpesvirus that establishes latency in the T cells of New World primates and has the ability to cause ... ...

Abstract	Viruses express several classes of non-coding RNAs; the functions and mechanisms by which most of these act are unknown. Herpesvirus saimiri, a γ-herpesvirus that establishes latency in the T cells of New World primates and has the ability to cause aggressive leukaemias and lymphomas in non-natural hosts, expresses seven small nuclear uracil-rich non-coding RNAs (called HSURs) in latently infected cells. These HSURs associate with Sm proteins, and share biogenesis and structural features with cellular Sm-class small nuclear RNAs. One of these HSURs (HSUR2) base-pairs with two host cellular microRNAs (miR-142-3p and miR-16) but does not affect their abundance or activity, which suggests that its interactions with them perform alternative functions. Here we show that HSUR2 also base-pairs with mRNAs in infected cells. We combined in vivo psoralen-mediated RNA-RNA crosslinking and high-throughput sequencing to identify the mRNAs targeted by HSUR2, which include mRNAs that encode retinoblastoma and factors involved in p53 signalling and apoptosis. We show that HSUR2 represses the expression of target mRNAs and that base-pairing between HSUR2 and miR-142-3p and miR-16 is essential for this repression, suggesting that HSUR2 recruits these two cellular microRNAs to its target mRNAs. Furthermore, we show that HSUR2 uses this mechanism to inhibit apoptosis. Our results uncover a role for this viral Sm-class RNA as a microRNA adaptor in the regulation of gene expression that follows precursor mRNA processing.
Language	English
Publishing date	2017-10-12
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature24034
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Depletion of the 26S proteasome adaptor Ecm29 increases Toll-like receptor 3 signaling.

Gorbea, Carlos / Rechsteiner, Martin / Vallejo, Jesús G / Bowles, Neil E

Science signaling

2013 Volume 6, Issue 295, Page(s) ra86

Abstract: Toll-like receptor 3 (TLR3) recognizes viral double-stranded RNA and stimulates the innate immune response. We found that depletion of extracellular mutant 29 (Ecm29), an adaptor protein that binds to a subset of 26S proteasomes (Ecm proteasomes), ... ...

Abstract	Toll-like receptor 3 (TLR3) recognizes viral double-stranded RNA and stimulates the innate immune response. We found that depletion of extracellular mutant 29 (Ecm29), an adaptor protein that binds to a subset of 26S proteasomes (Ecm proteasomes), increased the abundance of TLR3 in human embryonic kidney-293 and HeLa cells. Loss of Ecm29 also increased the amounts of LC3β and p62, two proteins that mediate autophagy. The absence of Ecm29 enhanced TLR3 signaling, which was characterized by the increased abundance of the adaptor protein and E3 ubiquitin ligase tumor necrosis factor receptor-associated factor 3, increased phosphorylation and activation of effector kinases downstream of TLR3, increased nuclear localization of the transcription factor interferon regulatory factor 3, and the accumulation of signaling molecules at juxtanuclear recycling endosomes. We conclude that Ecm proteasomes play a previously uncharacterized role in mediating autophagy, trafficking of TLR3, and attenuation of TLR3-dependent signaling.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/immunology ; Adaptor Proteins, Signal Transducing/metabolism ; Autophagy/genetics ; Autophagy/immunology ; HEK293 Cells ; HeLa Cells ; Humans ; Microtubule-Associated Proteins/biosynthesis ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/immunology ; Phosphorylation/genetics ; Phosphorylation/immunology ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/immunology ; Proteasome Endopeptidase Complex/metabolism ; Sequestosome-1 Protein ; Signal Transduction/genetics ; Signal Transduction/immunology ; Toll-Like Receptor 3/biosynthesis ; Toll-Like Receptor 3/genetics ; Toll-Like Receptor 3/immunology ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/immunology ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; ECPAS protein, human ; MAP1LC3B protein, human ; Microtubule-Associated Proteins ; SQSTM1 protein, human ; Sequestosome-1 Protein ; TLR3 protein, human ; Toll-Like Receptor 3 ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2013-10-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.2004301
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Differential transcriptional profiles identify microglial- and macrophage-specific gene markers expressed during virus-induced neuroinflammation.

DePaula-Silva, Ana Beatriz / Gorbea, Carlos / Doty, Daniel J / Libbey, Jane E / Sanchez, John Michael S / Hanak, Tyler J / Cazalla, Demián / Fujinami, Robert S

Journal of neuroinflammation

2019 Volume 16, Issue 1, Page(s) 152

Abstract: Background: In the healthy central nervous system (CNS), microglia are found in a homeostatic state and peripheral macrophages are absent from the brain. Microglia play key roles in maintaining CNS homeostasis and acting as first responders to infection ...

Abstract	Background: In the healthy central nervous system (CNS), microglia are found in a homeostatic state and peripheral macrophages are absent from the brain. Microglia play key roles in maintaining CNS homeostasis and acting as first responders to infection and inflammation, and peripheral macrophages infiltrate the CNS during neuroinflammation. Due to their distinct origins and functions, discrimination between these cell populations is essential to the comprehension of neuroinflammatory disorders. Studies comparing the gene profiles of microglia and peripheral macrophages, or macrophages in vitro-derived from bone marrow, under non-infectious conditions of the CNS, have revealed valuable microglial-specific genes. However, studies comparing gene profiles between CNS-infiltrating macrophages and microglia, when both are isolated from the CNS during viral-induced neuroinflammation, are lacking. Methods: We isolated, via flow cytometry, microglia and infiltrating macrophages from the brains of Theiler's murine encephalomyelitis virus-infected C57BL/6 J mice and used RNA-Seq, followed by validation with qPCR, to examine the differential transcriptional profiles of these cells. We utilized primary literature defining subcellular localization to determine whether or not particular proteins extracted from the transcriptional profiles were expressed at the cell surface. The surface expression and cellular specificity of triggering receptor expressed on myeloid cells 1 (TREM-1) protein were examined via flow cytometry. We also examined the immune response gene profile within the transcriptional profiles of these isolated microglia and infiltrating macrophages. Results: We have identified and validated new microglial- and macrophage-specific genes, encoding cell surface proteins, expressed at the peak of neuroinflammation. TREM-1 protein was confirmed to be expressed by infiltrating macrophages, not microglia, at the peak of neuroinflammation. We also identified both unique and redundant immune functions, through examination of the immune response gene profiles, of microglia and infiltrating macrophages during neurotropic viral infection. Conclusions: The differential expression of cell surface-specific genes during neuroinflammation can potentially be used to discriminate between microglia and macrophages as well as provide a resource that can be further utilized to target and manipulate specific cell responses during neuroinflammation.
MeSH term(s)	Animals ; Brain/immunology ; Cardiovirus Infections/immunology ; Inflammation/immunology ; Macrophages/immunology ; Mice ; Mice, Inbred C57BL ; Microglia/immunology ; Theilovirus/immunology ; Transcription, Genetic ; Transcriptome
Keywords	covid19
Language	English
Publishing date	2019-07-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2156455-3
ISSN	1742-2094 ; 1742-2094
ISSN (online)	1742-2094
ISSN	1742-2094
DOI	10.1186/s12974-019-1545-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Purification and assay of proteasome activator PA200.

Ustrell, Vicença / Pratt, Gregory / Gorbea, Carlos / Rechsteiner, Martin

Methods in enzymology

2005 Volume 398, Page(s) 321–329

Abstract: PA200, the most recently discovered activator of the 20S proteasome, is a nuclear protein thought to play a role in DNA repair. Homologs of PA200 have been found in rat, frog, birds, worms, and budding yeast, where it is called Blm3p (now known as Blm10p) ...

Abstract	PA200, the most recently discovered activator of the 20S proteasome, is a nuclear protein thought to play a role in DNA repair. Homologs of PA200 have been found in rat, frog, birds, worms, and budding yeast, where it is called Blm3p (now known as Blm10p), but not in Drosophila or fission yeast. Western blots of SDS-PAGE transfers reveal 160 and 200K forms of mammalian PA200, and organ surveys demonstrate that the 200K species is highest in testis. PA200 purified from bovine testis binds the ends of the cylindrical 20S proteasome, forming volcano-shaped structures in negatively stained EM images. In vitro assays demonstrate that binding of PA200 activates peptide hydrolysis by the 20S proteasome. This chapter describes the purification and assay of bovine testis PA200.
MeSH term(s)	Animals ; Cattle ; Centrifugation, Density Gradient/methods ; Chromatography, DEAE-Cellulose/methods ; Chromatography, Gel/methods ; Electrophoresis, Polyacrylamide Gel/methods ; Enzyme Activation/physiology ; Male ; Nuclear Proteins/analysis ; Nuclear Proteins/isolation & purification ; Nuclear Proteins/physiology ; Proteasome Endopeptidase Complex/metabolism ; Proteins ; Testis/chemistry ; Testis/metabolism
Chemical Substances	Nuclear Proteins ; Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2005
Publishing country	United States
Document type	Journal Article
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(05)98026-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Evidence that DNA replication is not regulated by ubiquitin-dependent proteolysis in Xenopus egg extract.

Mahaffey, David T / Gorbea, Carlos / Rechsteiner, Martin

Experimental cell research

2003 Volume 288, Issue 2, Page(s) 225–234

Abstract: The Xenopus early embryonic cell cycle consists of rapid oscillations between mitosis and DNA synthesis. We used ubiquitin (Ub)-dependent proteolysis inhibitors to determine whether Ub-mediated proteolysis regulates the initiation of DNA replication in ... ...

Abstract	The Xenopus early embryonic cell cycle consists of rapid oscillations between mitosis and DNA synthesis. We used ubiquitin (Ub)-dependent proteolysis inhibitors to determine whether Ub-mediated proteolysis regulates the initiation of DNA replication in Xenopus egg extract. Methylated Ub, a chemically modified Ub that cannot form chains, and S5a, a Ub chain-binding subunit of the 26S proteasome, were added to extract at concentrations known to inhibit cyclin B proteolysis and their effects on cell cycle progression and DNA replication were examined. DNA replication initiated concomitant with controls and proceeded in a semiconservative fashion in the presence of both methylated Ub and S5a. However, mitotic progression was halted, showing that the inhibitors were functional. We conclude that initiation of DNA replication is not regulated by Ub-dependent proteolysis in the early Xenopus cell cycle.
MeSH term(s)	Animals ; Aphidicolin/metabolism ; Carrier Proteins/metabolism ; Cyclin B/metabolism ; Cyclin B2 ; DNA Replication ; Enzyme Inhibitors/metabolism ; Humans ; Methylation ; Oocytes/metabolism ; Proteasome Endopeptidase Complex ; Tissue Extracts/metabolism ; Ubiquitin/chemistry ; Ubiquitin/metabolism ; Xenopus
Chemical Substances	CCNB2 protein, human ; Carrier Proteins ; Cyclin B ; Cyclin B2 ; Enzyme Inhibitors ; PSMD4 protein, human ; Tissue Extracts ; Ubiquitin ; Aphidicolin (38966-21-1) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2003-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/s0014-4827(03)00088-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 563: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: A Protein Interaction Network for Ecm29 Links the 26 S Proteasome to Molecular Motors and Endosomal Components

Gorbea, Carlos / Pratt, Gregory / Ustrell, Vicença / Bell, Russell / Sahasrabudhe, Sudhir / Hughes, Robert E / Rechsteiner, Martin

Journal of biological chemistry. 2010 Oct. 8, v. 285, no. 41

2010

Abstract: Ecm29 is a 200-kDa HEAT repeat protein that binds the 26 S proteasome. Genome-wide two-hybrid screens and mass spectrometry have identified molecular motors, endosomal components, and ubiquitin-proteasome factors as Ecm29-interacting proteins. The C- ... ...

Abstract	Ecm29 is a 200-kDa HEAT repeat protein that binds the 26 S proteasome. Genome-wide two-hybrid screens and mass spectrometry have identified molecular motors, endosomal components, and ubiquitin-proteasome factors as Ecm29-interacting proteins. The C-terminal half of human Ecm29 binds myosins and kinesins; its N-terminal region binds the endocytic proteins, Vps11, Rab11-FIP4, and rabaptin. Whereas full-length FLAG-Ecm29, its C-terminal half, and a small central fragment of Ecm29 remain bound to glycerol-gradient-separated 26 S proteasomes, the N-terminal half of Ecm29 does not. Confocal microscopy showed that Ecm-26 S proteasomes are present on flotillin-positive endosomes, but they are virtually absent from caveolin- and clathrin-decorated endosomes. Expression of the small central fragment of Ecm29 markedly reduces proteasome association with flotillin-positive endosomes. Identification of regions within Ecm29 capable of binding molecular motors, endosomal proteins, and the 26 S proteasome supports the hypothesis that Ecm29 serves as an adaptor for coupling 26 S proteasomes to specific cellular compartments.
Language	English
Dates of publication	2010-1008
Size	p. 31616-31633.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 65/118: Show issues
Z 6.2: Show issues

Order via subito

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.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components.

Gorbea, Carlos / Pratt, Gregory / Ustrell, Vicença / Bell, Russell / Sahasrabudhe, Sudhir / Hughes, Robert E / Rechsteiner, Martin

The Journal of biological chemistry

2010 Volume 285, Issue 41, Page(s) 31616–31633

Abstract	Ecm29 is a 200-kDa HEAT repeat protein that binds the 26 S proteasome. Genome-wide two-hybrid screens and mass spectrometry have identified molecular motors, endosomal components, and ubiquitin-proteasome factors as Ecm29-interacting proteins. The C-terminal half of human Ecm29 binds myosins and kinesins; its N-terminal region binds the endocytic proteins, Vps11, Rab11-FIP4, and rabaptin. Whereas full-length FLAG-Ecm29, its C-terminal half, and a small central fragment of Ecm29 remain bound to glycerol-gradient-separated 26 S proteasomes, the N-terminal half of Ecm29 does not. Confocal microscopy showed that Ecm-26 S proteasomes are present on flotillin-positive endosomes, but they are virtually absent from caveolin- and clathrin-decorated endosomes. Expression of the small central fragment of Ecm29 markedly reduces proteasome association with flotillin-positive endosomes. Identification of regions within Ecm29 capable of binding molecular motors, endosomal proteins, and the 26 S proteasome supports the hypothesis that Ecm29 serves as an adaptor for coupling 26 S proteasomes to specific cellular compartments.
MeSH term(s)	Animals ; Endosomes/genetics ; Endosomes/metabolism ; HeLa Cells ; Humans ; Mice ; Molecular Motor Proteins/genetics ; Molecular Motor Proteins/metabolism ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	ECPAS protein, human ; Molecular Motor Proteins ; VPS11 protein, human ; Vesicular Transport Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-) ; rab11 protein (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2010-08-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.154120
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito