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Article ; Online: Sphingolipids modulate docking, Ca

Abbineni, Prabhodh S / Coorssen, Jens R

The international journal of biochemistry & cell biology

2018 Volume 104, Page(s) 43–54

Abstract: Docking, priming, and membrane fusion of secretory vesicles (i.e. regulated exocytosis) requires lipids and proteins. Sphingolipids, in particular, sphingosine and sphingosine-1-phosphate, have been implicated in the modulation of exocytosis. However, ... ...

Abstract	Docking, priming, and membrane fusion of secretory vesicles (i.e. regulated exocytosis) requires lipids and proteins. Sphingolipids, in particular, sphingosine and sphingosine-1-phosphate, have been implicated in the modulation of exocytosis. However, the specific exocytotic steps that sphingolipids modulate and the enzymes that regulate sphingolipid concentrations on native secretory vesicle membranes remain unknown. Here we use tightly coupled functional and molecular analyses of fusion-ready cell surface complexes and cortical vesicles isolated from oocytes to assess the role of sphingolipids in the late, Ca
MeSH term(s)	Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Dose-Response Relationship, Drug ; Exocytosis/drug effects ; Humans ; Lysophospholipids/metabolism ; Membrane Fusion/drug effects ; Mice ; Phosphotransferases (Alcohol Group Acceptor)/chemistry ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Secretory Vesicles/drug effects ; Secretory Vesicles/metabolism ; Sphingolipids/metabolism ; Sphingosine/analogs & derivatives ; Sphingosine/metabolism
Chemical Substances	Lysophospholipids ; Sphingolipids ; sphingosine 1-phosphate (26993-30-6) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; sphingosine kinase 2, human (EC 2.7.1.91) ; Sphingosine (NGZ37HRE42) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-09-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2018.09.001
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Article ; Online: Application of High-Throughput Assays to Examine Phospho-Modulation of the Late Steps of Regulated Exocytosis.

Abbineni, Prabhodh S / Coorssen, Jens R

High-throughput

2017 Volume 6, Issue 4

Abstract: ... ...

Abstract	Abstract
Language	English
Publishing date	2017-11-13
Publishing country	Switzerland
Document type	Journal Article
ISSN	2571-5135
ISSN (online)	2571-5135
DOI	10.3390/ht6040017
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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: VAMP2 and synaptotagmin mobility in chromaffin granule membranes: implications for regulated exocytosis.

Abbineni, Prabhodh S / Briguglio, Joseph S / Chapman, Edwin R / Holz, Ronald W / Axelrod, Daniel

Molecular biology of the cell

2021 Volume 33, Issue 6, Page(s) ar53

Abstract: Granule-plasma membrane docking and fusion can only occur when proteins that enable these reactions are present at the granule-plasma membrane contact. Thus, the mobility of granule membrane proteins may influence docking and membrane fusion. We measured ...

Abstract	Granule-plasma membrane docking and fusion can only occur when proteins that enable these reactions are present at the granule-plasma membrane contact. Thus, the mobility of granule membrane proteins may influence docking and membrane fusion. We measured the mobility of vesicle associated membrane protein 2 (VAMP2), synaptotagmin 1 (Syt1), and synaptotagmin 7 (Syt7) in chromaffin granule membranes in living chromaffin cells. We used a method that is not limited by standard optical resolution. A bright flash of strongly decaying evanescent field produced by total internal reflection was used to photobleach GFP-labeled proteins in the granule membrane. Fluorescence recovery occurs as unbleached protein in the granule membrane distal from the glass interface diffuses into the more bleached proximal regions, enabling the measurement of diffusion coefficients. We found that VAMP2-EGFP and Syt7-EGFP are mobile with a diffusion coefficient of ∼3 × 10
MeSH term(s)	Calcium/metabolism ; Chromaffin Cells/metabolism ; Chromaffin Granules/metabolism ; Exocytosis ; Membrane Fusion ; Synaptotagmin I/metabolism ; Vesicle-Associated Membrane Protein 2/metabolism
Chemical Substances	Synaptotagmin I ; Vesicle-Associated Membrane Protein 2 ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-12-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E21-10-0494
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Zs.A 2853: 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)
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Article ; Online: Visualization of expanding fusion pores in secretory cells.

Abbineni, Prabhodh S / Axelrod, Daniel / Holz, Ronald W

The Journal of general physiology

2018 Volume 150, Issue 12, Page(s) 1640–1646

MeSH term(s)	Animals ; Chromaffin Cells/physiology ; Exocytosis ; Green Fluorescent Proteins ; Humans ; Molecular Imaging ; Pleckstrin Homology Domains
Chemical Substances	Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2018-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.201812186
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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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Zs.A 389: Show issues

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Article ; Online: Chromogranin A, the major lumenal protein in chromaffin granules, controls fusion pore expansion.

Abbineni, Prabhodh S / Bittner, Mary A / Axelrod, Daniel / Holz, Ronald W

The Journal of general physiology

2018 Volume 151, Issue 2, Page(s) 118–130

Abstract: Upon fusion of the secretory granule with the plasma membrane, small molecules are discharged through the immediately formed narrow fusion pore, but protein discharge awaits pore expansion. Recently, fusion pore expansion was found to be regulated by ... ...

Abstract	Upon fusion of the secretory granule with the plasma membrane, small molecules are discharged through the immediately formed narrow fusion pore, but protein discharge awaits pore expansion. Recently, fusion pore expansion was found to be regulated by tissue plasminogen activator (tPA), a protein present within the lumen of chromaffin granules in a subpopulation of chromaffin cells. Here, we further examined the influence of other lumenal proteins on fusion pore expansion, especially chromogranin A (CgA), the major and ubiquitous lumenal protein in chromaffin granules. Polarized TIRF microscopy demonstrated that the fusion pore curvature of granules containing CgA-EGFP was long lived, with curvature lifetimes comparable to those of tPA-EGFP-containing granules. This was surprising because fusion pore curvature durations of granules containing exogenous neuropeptide Y-EGFP (NPY-EGFP) are significantly shorter (80% lasting <1 s) than those containing CgA-EGFP, despite the anticipated expression of endogenous CgA. However, quantitative immunocytochemistry revealed that transiently expressed lumenal proteins, including NPY-EGFP, caused a down-regulation of endogenously expressed proteins, including CgA. Fusion pore curvature durations in nontransfected cells were significantly longer than those of granules containing overexpressed NPY but shorter than those associated with granules containing overexpressed tPA, CgA, or chromogranin B. Introduction of CgA to NPY-EGFP granules by coexpression converted the fusion pore from being transient to being longer lived, comparable to that found in nontransfected cells. These findings demonstrate that several endogenous chromaffin granule lumenal proteins are regulators of fusion pore expansion and that alteration of chromaffin granule contents affects fusion pore lifetimes. Importantly, the results indicate a new role for CgA. In addition to functioning as a prohormone, CgA plays an important role in controlling fusion pore expansion.
MeSH term(s)	Animals ; Cattle ; Cells, Cultured ; Chromaffin Cells/metabolism ; Chromogranin A/metabolism ; Membrane Fusion ; Neuropeptide Y/metabolism ; Secretory Pathway ; Secretory Vesicles/metabolism ; Tissue Plasminogen Activator/metabolism
Chemical Substances	Chromogranin A ; Neuropeptide Y ; Tissue Plasminogen Activator (EC 3.4.21.68)
Language	English
Publishing date	2018-11-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.201812182
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Article ; Online: Identification of β-synuclein on secretory granules in chromaffin cells and the effects of α- and β-synuclein on post-fusion BDNF discharge and fusion pore expansion.

Abbineni, Prabhodh S / Bohannon, Kevin P / Bittner, Mary A / Axelrod, Daniel / Holz, Ronald W

Neuroscience letters

2019 Volume 699, Page(s) 134–139

Abstract: α-Synuclein is strongly implicated in the pathogenesis of Parkinson's disease as well as in other neurodegenerative diseases. However, its normal function in cells is not understood. The N-termini of α-, β-, and γ-synuclein contains six to seven 11-amino ...

Abstract	α-Synuclein is strongly implicated in the pathogenesis of Parkinson's disease as well as in other neurodegenerative diseases. However, its normal function in cells is not understood. The N-termini of α-, β-, and γ-synuclein contains six to seven 11-amino acid repeats that are predicted to form amphipathic helices. Membrane-binding and membrane-curving abilities of synuclein raise the possibility that synuclein could alter cellular processes that involve highly curved structures. In the present study we examined the localization of endogenous synuclein in bovine chromaffin cells by immunocytochemistry and its possible function to control protein discharge upon fusion of the granule with the plasma membrane by regulating the fusion pore. We found with quantitative immunocytochemistry that endogenous β-synuclein associates with secretory granules. Endogenous α-synuclein only rarely co-localizes with secretory granules. Overexpression of α-synuclein but not β-synuclein quickened the post- fusion discharge of BDNF-pHluorin by approxinately 30%. However, neither α- nor β-synuclein significantly altered curvature dynamics associated with fusion pore expansion that were measured by the combination of polarization and total internal reflection fluorescence microscopy (pTIRFM). Whatever the mechanism, the physiological significance of the small increased rate of post-fusion protein discharge caused by α-synuclein remains to be demonstrated, especially since endogenous β-, but not α-synuclein is the predominant synuclein isoform associated with chromaffin granules.
MeSH term(s)	Animals ; Brain-Derived Neurotrophic Factor/metabolism ; Cattle ; Cells, Cultured ; Chromaffin Cells/metabolism ; Exocytosis/physiology ; Green Fluorescent Proteins/metabolism ; Porosity ; Secretory Vesicles/metabolism ; alpha-Synuclein/metabolism ; beta-Synuclein/metabolism
Chemical Substances	Brain-Derived Neurotrophic Factor ; PHluorin ; alpha-Synuclein ; beta-Synuclein ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2019-01-31
Publishing country	Ireland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	194929-9
ISSN	1872-7972 ; 0304-3940
ISSN (online)	1872-7972
ISSN	0304-3940
DOI	10.1016/j.neulet.2019.01.056
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