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Article ; Online: Cargo selection in endoplasmic reticulum-to-Golgi transport and relevant diseases.

Tang, Vi T / Ginsburg, David

2023 Volume 133, Issue 1

Abstract: Most proteins destined for the extracellular space or various intracellular compartments must traverse the intracellular secretory pathway. The first step is the recruitment and transport of cargoes from the endoplasmic reticulum (ER) lumen to the Golgi ... ...

Abstract	Most proteins destined for the extracellular space or various intracellular compartments must traverse the intracellular secretory pathway. The first step is the recruitment and transport of cargoes from the endoplasmic reticulum (ER) lumen to the Golgi apparatus by coat protein complex II (COPII), consisting of five core proteins. Additional ER transmembrane proteins that aid cargo recruitment are referred to as cargo receptors. Gene duplication events have resulted in multiple COPII paralogs present in the mammalian genome. Here, we review the functions of each COPII protein, human disorders associated with each paralog, and evidence for functional conservation between paralogs. We also provide a summary of current knowledge regarding two prototypical cargo receptors in mammals, LMAN1 and SURF4, and their roles in human health and disease.
MeSH term(s)	Animals ; Humans ; Protein Transport ; COP-Coated Vesicles/genetics ; COP-Coated Vesicles/metabolism ; Biological Transport/physiology ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/genetics ; Golgi Apparatus/metabolism ; Mammals/metabolism
Chemical Substances	Membrane Proteins ; SURF4 protein, human
Language	English
Publishing date	2023-01-03
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI163838
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Article ; Online: Identification of LMAN1- and SURF4-Dependent Secretory Cargoes.

Tang, Vi T / Abbineni, Prabhodh S / Veiga Leprevost, Felipe da / Basrur, Venkatesha / Khoriaty, Rami / Emmer, Brian T / Nesvizhskii, Alexey I / Ginsburg, David

Journal of proteome research

2023 Volume 22, Issue 11, Page(s) 3439–3446

Abstract: Most proteins secreted into the extracellular space are first recruited from the endoplasmic reticulum into coat protein complex II (COPII)-coated vesicles or tubules that facilitate their transport to the Golgi apparatus. Although several secreted ... ...

Abstract	Most proteins secreted into the extracellular space are first recruited from the endoplasmic reticulum into coat protein complex II (COPII)-coated vesicles or tubules that facilitate their transport to the Golgi apparatus. Although several secreted proteins have been shown to be actively recruited into COPII vesicles and tubules by the cargo receptors LMAN1 and SURF4, the full cargo repertoire of these receptors is unknown. We now report mass spectrometry analysis of conditioned media and cell lysates from HuH7 cells CRISPR targeted to inactivate the
MeSH term(s)	Humans ; Carrier Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus ; Membrane Proteins/metabolism ; Protein Transport
Chemical Substances	Carrier Proteins ; Membrane Proteins ; SURF4 protein, human
Language	English
Publishing date	2023-10-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.3c00259
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Article: Identification of LMAN1 and SURF4 dependent secretory cargoes.

Tang, Vi T / Abbineni, Prabhodh S / Leprevost, Felipe da Veiga / Basrur, Venkatesha / Emmer, Brian T / Nesvizhskii, Alexey I / Ginsburg, David

bioRxiv : the preprint server for biology

2023

Abstract	Most proteins secreted into the extracellular space are first recruited from the endoplasmic reticulum into coat protein complex II (COPII)-coated vesicles or tubules that facilitate their transport to the Golgi apparatus. Although several secreted proteins have been shown to be actively recruited into COPII vesicles/tubules by the cargo receptors LMAN1 and SURF4, the full cargo repertoire of these receptors is unknown. We now report mass spectrometry analysis of conditioned media and cell lysates from HuH7 cells CRISPR targeted to inactivate the
Language	English
Publishing date	2023-04-06
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.04.06.535922
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Article: Functional overlap between the mammalian

Tang, Vi T / Xiang, Jie / Chen, Zhimin / McCormick, Joseph / Abbineni, Prabhodh S / Chen, Xiao-Wei / Hoenerhoff, Mark / Emmer, Brian T / Khoriaty, Rami / Lin, Jiandie D / Ginsburg, David

bioRxiv : the preprint server for biology

2024

Abstract: Proteins carrying a signal peptide and/or a transmembrane domain enter the intracellular secretory pathway at the endoplasmic reticulum (ER) and are transported to the Golgi apparatus via COPII vesicles or tubules. SAR1 initiates COPII coat assembly by ... ...

Abstract	Proteins carrying a signal peptide and/or a transmembrane domain enter the intracellular secretory pathway at the endoplasmic reticulum (ER) and are transported to the Golgi apparatus via COPII vesicles or tubules. SAR1 initiates COPII coat assembly by recruiting other coat proteins to the ER membrane. Mammalian genomes encode two
Language	English
Publishing date	2024-02-29
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.02.27.582310
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Article ; Online: Identification of secreted proteins by comparison of protein abundance in conditioned media and cell lysates.

Abbineni, Prabhodh S / Tang, Vi T / da Veiga Leprevost, Felipe / Basrur, Venkatesha / Xiang, Jie / Nesvizhskii, Alexey I / Ginsburg, David

Analytical biochemistry

2022 Volume 655, Page(s) 114846

Abstract: Analysis of the full spectrum of secreted proteins in cell culture is complicated by leakage of intracellular proteins from damaged cells. To address this issue, we compared the abundance of individual proteins between the cell lysate and the conditioned ...

Abstract	Analysis of the full spectrum of secreted proteins in cell culture is complicated by leakage of intracellular proteins from damaged cells. To address this issue, we compared the abundance of individual proteins between the cell lysate and the conditioned medium, reasoning that secreted proteins should be relatively more abundant in the conditioned medium. Marked enrichment for signal-peptide-bearing proteins with increasing conditioned media to cell lysate ratio, as well loss of this signal following brefeldin A treatment, confirmed the sensitivity and specificity of this approach. The subset of proteins demonstrating increased conditioned media to cell lysate ratio in the presence of Brefeldin A identified candidates for unconventional secretion via a pathway independent of ER to Golgi trafficking.
MeSH term(s)	Brefeldin A/metabolism ; Brefeldin A/pharmacology ; Culture Media, Conditioned/metabolism ; Golgi Apparatus/metabolism ; Proteins/metabolism
Chemical Substances	Culture Media, Conditioned ; Proteins ; Brefeldin A (20350-15-6)
Language	English
Publishing date	2022-08-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2022.114846
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Article ; Online: Whole-Exome Sequencing Reveals

Tang, Vi T / Arscott, Patricia / Helms, Adam S / Day, Sharlene M

Circulation. Genomic and precision medicine

2018 Volume 11, Issue 1, Page(s) e001966

MeSH term(s)	Amino Acid Sequence ; Atrial Natriuretic Factor/genetics ; Cell Nucleus/metabolism ; DNA Mutational Analysis ; GATA4 Transcription Factor/chemistry ; GATA4 Transcription Factor/genetics ; GATA4 Transcription Factor/metabolism ; HEK293 Cells ; Heart Defects, Congenital/diagnosis ; Heart Defects, Congenital/genetics ; Humans ; Male ; Middle Aged ; PTEN Phosphohydrolase/chemistry ; PTEN Phosphohydrolase/genetics ; PTEN Phosphohydrolase/metabolism ; Pedigree ; Ultrasonography ; Whole Exome Sequencing ; Young Adult
Chemical Substances	GATA4 Transcription Factor ; GATA4 protein, human ; Atrial Natriuretic Factor (85637-73-6) ; PTEN Phosphohydrolase (EC 3.1.3.67) ; PTEN protein, human (EC 3.1.3.67)
Language	English
Publishing date	2018-01-12
Publishing country	United States
Document type	Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2574-8300
ISSN (online)	2574-8300
DOI	10.1161/CIRCGEN.117.001966
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Article ; Online: Hepatic inactivation of murine <i>Surf4</i> results in marked reduction in plasma cholesterol.

Tang, Vi T / McCormick, Joseph / Xu, Bolin / Wang, Yawei / Fang, Huan / Wang, Xiao / Siemieniak, David / Khoriaty, Rami / Emmer, Brian T / Chen, Xiao-Wei / Ginsburg, David

eLife

2022 Volume 11

Abstract: PCSK9 negatively regulates low-density lipoprotein receptor (LDLR) abundance on the cell surface, leading to decreased hepatic clearance of LDL particles and increased levels of plasma cholesterol. We previously identified SURF4 as a cargo receptor that ... ...

Abstract	PCSK9 negatively regulates low-density lipoprotein receptor (LDLR) abundance on the cell surface, leading to decreased hepatic clearance of LDL particles and increased levels of plasma cholesterol. We previously identified SURF4 as a cargo receptor that facilitates PCSK9 secretion in HEK293T cells (Emmer et al., 2018). Here, we generated hepatic SURF4-deficient mice (Surf4<sup>fl/fl</sup> Alb-Cre<sup>+</sup>) to investigate the physiologic role of SURF4 in vivo. Surf4<sup>fl/fl</sup> Alb-Cre<sup>+</sup> mice exhibited normal viability, gross development, and fertility. Plasma PCSK9 levels were reduced by ~60% in Surf4<sup>fl/fl</sup> Alb-Cre<sup>+</sup> mice, with a corresponding ~50% increase in steady state LDLR protein abundance in the liver, consistent with SURF4 functioning as a cargo receptor for PCSK9. Surprisingly, these mice exhibited a marked reduction in plasma cholesterol and triglyceride levels out of proportion to the partial increase in hepatic LDLR abundance. Detailed characterization of lipoprotein metabolism in these mice instead revealed a severe defect in hepatic lipoprotein secretion, consistent with prior reports of SURF4 also promoting the secretion of apolipoprotein B (APOB). Despite a small increase in liver mass and lipid content, histologic evaluation revealed no evidence of steatohepatitis or fibrosis in Surf4<sup>fl/fl</sup> Alb-Cre<sup>+</sup> mice. Acute depletion of hepatic SURF4 by CRISPR/Cas9 or liver-targeted siRNA in adult mice confirms these findings. Together, these data support the physiologic significance of SURF4 in the hepatic secretion of PCSK9 and APOB-containing lipoproteins and its potential as a therapeutic target in atherosclerotic cardiovascular diseases.
MeSH term(s)	Mice ; Humans ; Animals ; Proprotein Convertase 9/genetics ; Proprotein Convertase 9/metabolism ; RNA, Small Interfering/metabolism ; HEK293 Cells ; Mice, Inbred C57BL ; Receptors, LDL/genetics ; Receptors, LDL/metabolism ; Liver/metabolism ; Apolipoproteins B/metabolism ; Lipoproteins/metabolism ; Triglycerides/metabolism ; Cholesterol/metabolism ; Lipoproteins, LDL/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism
Chemical Substances	PCSK9 protein, human (EC 3.4.21.-) ; Proprotein Convertase 9 (EC 3.4.21.-) ; RNA, Small Interfering ; Receptors, LDL ; Apolipoproteins B ; Lipoproteins ; Triglycerides ; Cholesterol (97C5T2UQ7J) ; Lipoproteins, LDL ; SURF4 protein, human ; Membrane Proteins ; Surf4 protein, mouse
Language	English
Publishing date	2022-10-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.82269
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Identification of cell type specific ACE2 modifiers by CRISPR screening.

Sherman, Emily J / Mirabelli, Carmen / Tang, Vi T / Khan, Taslima G / Leix, Kyle / Kennedy, Andrew A / Graham, Sarah E / Willer, Cristen J / Tai, Andrew W / Sexton, Jonathan Z / Wobus, Christiane E / Emmer, Brian T

PLoS pathogens

2022 Volume 18, Issue 3, Page(s) e1010377

Abstract: SARS-CoV-2 infection is initiated by binding of the viral spike protein to its receptor, ACE2, on the surface of host cells. ACE2 expression is heterogeneous both in vivo and in immortalized cell lines, but the molecular pathways that govern ACE2 ... ...

Abstract	SARS-CoV-2 infection is initiated by binding of the viral spike protein to its receptor, ACE2, on the surface of host cells. ACE2 expression is heterogeneous both in vivo and in immortalized cell lines, but the molecular pathways that govern ACE2 expression remain unclear. We now report high-throughput CRISPR screens for functional modifiers of ACE2 surface abundance. In liver-derived HuH7 cells, we identified 35 genes whose disruption was associated with a change in the surface abundance of ACE2. Enriched among these ACE2 regulators were established transcription factors, epigenetic regulators, and functional networks. We further characterized individual HuH7 cell lines with disruption of SMAD4, EP300, PIAS1, or BAMBI and found these genes to regulate ACE2 at the mRNA level and to influence cellular susceptibility to SARS-CoV-2 infection. Orthogonal screening of lung-derived Calu-3 cells revealed a distinct set of ACE2 modifiers comprised of ACE2, KDM6A, MOGS, GPAA1, and UGP2. Collectively, our findings clarify the host factors involved in SARS-CoV-2 entry, highlight the cell type specificity of ACE2 regulatory networks, and suggest potential targets for therapeutic development.
MeSH term(s)	Angiotensin-Converting Enzyme 2/genetics ; COVID-19/genetics ; Cell Line ; Clustered Regularly Interspaced Short Palindromic Repeats ; Humans ; SARS-CoV-2/genetics ; Spike Glycoprotein, Coronavirus/metabolism
Chemical Substances	Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2022-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010377
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Article ; Online: Murine Surf4 is essential for early embryonic development.

Emmer, Brian T / Lascuna, Paul J / Tang, Vi T / Kotnik, Emilee N / Saunders, Thomas L / Khoriaty, Rami / Ginsburg, David

PloS one

2020 Volume 15, Issue 1, Page(s) e0227450

Abstract: Newly synthesized proteins co-translationally inserted into the endoplasmic reticulum (ER) lumen may be recruited into anterograde transport vesicles by their association with specific cargo receptors. We recently identified a role for the cargo receptor ...

Abstract	Newly synthesized proteins co-translationally inserted into the endoplasmic reticulum (ER) lumen may be recruited into anterograde transport vesicles by their association with specific cargo receptors. We recently identified a role for the cargo receptor SURF4 in facilitating the secretion of PCSK9 in cultured cells. To examine the function of SURF4 in vivo, we used CRISPR/Cas9-mediated gene editing to generate mice with germline loss-of-function mutations in Surf4. Heterozygous Surf4+/- mice exhibit grossly normal appearance, behavior, body weight, fecundity, and organ development, with no significant alterations in circulating plasma levels of PCSK9, apolipoprotein B, or total cholesterol, and a detectable accumulation of intrahepatic apoliprotein B. Homozygous Surf4-/- mice exhibit embryonic lethality, with complete loss of all Surf4-/- offspring between embryonic days 3.5 and 9.5. In contrast to the milder murine phenotypes associated with deficiency of known SURF4 cargoes, the embryonic lethality of Surf4-/- mice implies the existence of additional SURF4 cargoes or functions that are essential for murine early embryonic development.
MeSH term(s)	Alleles ; Animals ; Apolipoproteins B/blood ; Apolipoproteins B/metabolism ; CRISPR-Cas Systems/genetics ; Cholesterol/blood ; Embryonic Development ; Gene Editing ; Heterozygote ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Knockout ; Proprotein Convertase 9/blood ; Proprotein Convertase 9/metabolism
Chemical Substances	Apolipoproteins B ; Membrane Proteins ; Surf4 protein, mouse ; Cholesterol (97C5T2UQ7J) ; Proprotein Convertase 9 (EC 3.4.21.-)
Language	English
Publishing date	2020-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0227450
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Article: Identification of ACE2 modifiers by CRISPR screening.

Sherman, Emily J / Mirabelli, Carmen / Tang, Vi T / Khan, Taslima G / Kennedy, Andrew A / Graham, Sarah E / Willer, Cristen J / Tai, Andrew W / Sexton, Jonathan Z / Wobus, Christiane E / Emmer, Brian T

bioRxiv : the preprint server for biology

2021

Abstract: SARS-CoV-2 infection is initiated by binding of the viral spike protein to its receptor, ACE2, on the surface of host cells. ACE2 expression is heterogeneous ... ...

Abstract	SARS-CoV-2 infection is initiated by binding of the viral spike protein to its receptor, ACE2, on the surface of host cells. ACE2 expression is heterogeneous both
Language	English
Publishing date	2021-06-10
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.06.10.447768
Database	MEDical Literature Analysis and Retrieval System OnLINE

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