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Article ; Online: A junction-dependent mechanism drives murine mammary cell intercalation for ductal elongation.

Pfannenstein, Alexander / Macara, Ian G

2023 Volume 58, Issue 13, Page(s) 1126–1138.e4

Abstract: The luminal epithelium of the mammary gland is organized into monolayers; however, it originates from multilayered terminal end buds (TEBs) during development. Although apoptosis provides a plausible mechanism for cavitation of the ductal lumen, it doesn' ...

Abstract	The luminal epithelium of the mammary gland is organized into monolayers; however, it originates from multilayered terminal end buds (TEBs) during development. Although apoptosis provides a plausible mechanism for cavitation of the ductal lumen, it doesn't account for ductal elongation behind TEBs. Spatial calculations in mice suggest that most TEB cells integrate into the outermost luminal layer to generate elongation. We developed a quantitative cell culture assay that models intercalation into epithelial monolayers. We found that tight junction proteins play a key role in this process. ZO-1 puncta form at the new cellular interface and resolve into a new boundary as intercalation proceeds. Deleting ZO-1 suppresses intercalation both in culture and in cells transplanted into mammary glands via intraductal injection. Cytoskeletal rearrangements at the interface are critical for intercalation. These data identify luminal cell rearrangements necessary for mammary development and suggest a mechanism for integration of cells into an existing monolayer.
MeSH term(s)	Mice ; Animals ; Mammary Glands, Animal ; Epithelium
Language	English
Publishing date	2023-05-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2023.04.009
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Article: Mammalian Pins is a conformational switch that links NuMA to heterotrimeric G proteins.

Du, Quansheng / Macara, Ian G

Cell

2004 Volume 119, Issue 4, Page(s) 503–516

Abstract: ... In invertebrates, spindle positioning requires Pins or related proteins and a G protein alpha subunit. A mammalian ...

Abstract	During asymmetric cell divisions, mitotic spindles align along the axis of polarization. In invertebrates, spindle positioning requires Pins or related proteins and a G protein alpha subunit. A mammalian Pins, called LGN, binds Galphai and also interacts through an N-terminal domain with the microtubule binding protein NuMA. During mitosis, LGN recruits NuMA to the cell cortex, while cortical association of LGN itself requires the C-terminal Galpha binding domain. Using a FRET biosensor, we find that LGN behaves as a conformational switch: in its closed state, the N and C termini interact, but NuMA or Galphai can disrupt this association, allowing LGN to interact simultaneously with both proteins, resulting in their cortical localization. Overexpression of Galphai or YFP-LGN causes a pronounced oscillation of metaphase spindles, and NuMA binding to LGN is required for these spindle movements. We propose that a related switch mechanism might operate in asymmetric cell divisions in the fly and nematode.
MeSH term(s)	Animals ; Antigens, Nuclear ; Carrier Proteins/metabolism ; Cell Cycle ; Cell Line ; Cell Line, Transformed ; Cell Polarity ; Chromosomes/physiology ; Dogs ; Fluorescence Resonance Energy Transfer ; GTP-Binding Protein alpha Subunits ; Heterotrimeric GTP-Binding Proteins ; Intracellular Signaling Peptides and Proteins ; Microtubules/physiology ; Models, Biological ; Nuclear Matrix-Associated Proteins ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Conformation ; Saccharomyces cerevisiae ; Spindle Apparatus/physiology ; Transfection
Chemical Substances	Antigens, Nuclear ; Carrier Proteins ; GPSM2 protein, human ; GTP-Binding Protein alpha Subunits ; Intracellular Signaling Peptides and Proteins ; NUMA1 protein, human ; Nuclear Matrix-Associated Proteins ; Nuclear Proteins ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1)
Language	English
Publishing date	2004-11-12
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2004.10.028
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Zs.A 1167: 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)
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Article: A Size Filter Regulates Apical Protein Sorting.

de Caestecker, Christian / Macara, Ian G

Research square

2023

Abstract: Despite decades of research, apical sorting of epithelial membrane proteins remains incompletely understood. We noted that apical cytoplasmic domains are smaller than those of basolateral proteins; however, the reason for this discrepancy is unknown. We ... ...

Abstract	Despite decades of research, apical sorting of epithelial membrane proteins remains incompletely understood. We noted that apical cytoplasmic domains are smaller than those of basolateral proteins; however, the reason for this discrepancy is unknown. We investigated whether a size barrier at the trans-Golgi network (TGN) might hinder apical sorting of proteins with large cytoplasmic tails. We focused on Crb3 and Ace2 as representative apical proteins with short cytoplasmic tails. By incorporating a streptavidin-binding peptide, these proteins can be trapped in the endoplasmic reticulum (ER) until addition of biotin, which triggers synchronous release to the Golgi and subsequent transport to the apical cortex. Strikingly, departure from the Golgi could be significantly delayed simply by increasing cytoplasmic bulk. Moreover, large and small Crb3 segregated into spatially distinct Golgi regions as detected by super resolution imaging. Biologically, Crb3 forms a complex through its cytoplasmic tail with the Pals1 protein, which could also delay departure, but although associated at the ER and Golgi, we found that Pals1 disassociates prior to Crb3 departure. Notably, a non-dissociable mutant Pals1 hampers the exit of Crb3. We conclude that an unexpected mechanism involving a size filter at the TGN facilitates apical sorting of proteins with small cytoplasmic domains and that timely release of Pals1, to reduce cytoplasmic domain size, is essential for the normal kinetics of Crb3 sorting.
Language	English
Publishing date	2023-08-04
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-3210598/v1
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Article: Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G-protein beta gamma subunits.

Mattingly, R R / Macara, I G

Nature

1996 Volume 382, Issue 6588, Page(s) 268–272

Abstract: ... dependent increases in exchange-factor activity, whereas cotransfection with G-protein beta gamma subunits ... caused a constitutive activation that was sensitive to PP1. These results demonstrate a G-protein-coupled ...

Abstract	Muscarinic receptors activate Ras through a pathway distinct from that mediated through translocation of the exchange factor mSos1 by receptor tyrosine kinases. Here we report that muscarinic receptors can activate another Ras exchange factor, CDC25Mm, or p140Ras-GRF (refs 5,6). In NIH-3T3 cells expressing subtype 1 human muscarinic receptors (hm1), the agonist carbachol selectively increased the specific activity and phosphorylation state of epitope-tagged Ras-GRF. This stimulation was reversed by protein phosphatase 1 (PP1), and prevented by transducin alpha-subunits. Carbachol treatment of neonatal rat brain explants increasd Ras exchange factor activity and the phosphorylation state of endogenous Ras-GRF. In COS-7 cells, cotransfection of hm1 or hm2 receptors with Ras-GRF conferred carbachol-dependent increases in exchange-factor activity, whereas cotransfection with G-protein beta gamma subunits caused a constitutive activation that was sensitive to PP1. These results demonstrate a G-protein-coupled mechanism for Ras activation, mediated by p140 Ras-GRF.
MeSH term(s)	3T3 Cells ; Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/drug effects ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Carbachol/pharmacology ; Cloning, Molecular ; Enzyme Activation ; Epidermal Growth Factor/metabolism ; GTP-Binding Proteins/metabolism ; Guanine Nucleotide Exchange Factors ; Humans ; Mice ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Phosphatase 1 ; Proteins/genetics ; Proteins/metabolism ; Rats ; Receptors, Muscarinic/metabolism ; Recombinant Proteins/metabolism ; ras Guanine Nucleotide Exchange Factors ; ras Proteins/metabolism ; ras-GRF1
Chemical Substances	Guanine Nucleotide Exchange Factors ; Proteins ; Receptors, Muscarinic ; Recombinant Proteins ; ras Guanine Nucleotide Exchange Factors ; ras-GRF1 ; Epidermal Growth Factor (62229-50-9) ; Carbachol (8Y164V895Y) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Protein Phosphatase 1 (EC 3.1.3.16) ; GTP-Binding Proteins (EC 3.6.1.-) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	1996-07-18
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/382268a0
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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)
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Article ; Online: Stem cell conversion to the cardiac lineage requires nucleotide signalling from apoptosing cells.

Fort, Loic / Gama, Vivian / Macara, Ian G

Nature cell biology

2022 Volume 24, Issue 4, Page(s) 434–447

Abstract: Pluripotent stem cells can be driven by manipulation of Wnt signalling through a series of states similar to those that occur during early embryonic development, transitioning from an epithelial phenotype into the cardiogenic-mesoderm lineage and ... ...

Abstract	Pluripotent stem cells can be driven by manipulation of Wnt signalling through a series of states similar to those that occur during early embryonic development, transitioning from an epithelial phenotype into the cardiogenic-mesoderm lineage and ultimately into functional cardiomyocytes. Strikingly, we observed that initiation of differentiation in induced pluripotent stem cells (iPSCs) and embryonic stem cells triggers widespread apoptosis, followed by a synchronous epithelial-mesenchymal transition (EMT). Apoptosis is caused by the absence of bFGF in the differentiation medium. EMT requires induction of the transcription factors SNAI1 and SNAI2 downstream of MESP1 expression, and double knockout of SNAI1 and SNAI2 or loss of MESP1 in iPSCs blocks EMT and prevents cardiac differentiation. Remarkably, blockade of early apoptosis, either chemically or by ablation of pro-apoptotic genes, also completely prevents EMT, suppressing even the earliest events in mesoderm conversion, including T/BRA, TBX6 and MESP1 induction. Conditioned medium from WNT-activated wild-type iPSCs overcomes the block to EMT by cells incapable of apoptosis, suggesting involvement of soluble factors from apoptotic cells in mesoderm conversion. Knockout of the PANX1 channel blocked EMT, whereas treatment with a purinergic P2-receptor inhibitor or addition of apyrase demonstrated a requirement for nucleotide triphosphate signalling. ATP and/or UTP was sufficient to induce a partial EMT in apoptosis-incapable cells treated with WNT activator. Notably, knockout of the ATP/UTP-specific P2Y2 receptor blocked EMT and mesoderm induction. We conclude that in addition to acting as chemo-attractants for clearance of apoptotic cells, nucleotides can function as essential paracrine signals that, with WNT signalling, create a logical AND gate for mesoderm specification.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Apoptosis ; Basic Helix-Loop-Helix Transcription Factors/metabolism ; Cell Differentiation/genetics ; Embryonic Stem Cells/metabolism ; Mesoderm ; Nucleotides/metabolism ; Uridine Triphosphate/metabolism ; Wnt Signaling Pathway
Chemical Substances	Basic Helix-Loop-Helix Transcription Factors ; Nucleotides ; Adenosine Triphosphate (8L70Q75FXE) ; Uridine Triphosphate (UT0S826Z60)
Language	English
Publishing date	2022-04-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-022-00888-x
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Zs.A 5169: 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: Genome-wide CRISPR screen identifies noncanonical NF-κB signaling as a regulator of density-dependent proliferation.

Fomicheva, Maria / Macara, Ian G

eLife

2020 Volume 9

Abstract: Epithelial cells possess intrinsic mechanisms to maintain an appropriate cell density for normal tissue morphogenesis and homeostasis. Defects in such mechanisms likely contribute to hyperplasia and cancer initiation. To identify genes that regulate the ... ...

Abstract	Epithelial cells possess intrinsic mechanisms to maintain an appropriate cell density for normal tissue morphogenesis and homeostasis. Defects in such mechanisms likely contribute to hyperplasia and cancer initiation. To identify genes that regulate the density-dependent proliferation of murine mammary epithelial cells, we developed a fluorescence-activated cell sorting assay based on fluorescence ubiquitination cell cycle indicator, which marks different stages of the cell cycle with distinct fluorophores. Using this powerful assay, we performed a genome-wide CRISPR/Cas9 knockout screen, selecting for cells that proliferate normally at low density but continue to divide at high density. Unexpectedly, one top hit was
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line ; Cell Proliferation/physiology ; Clustered Regularly Interspaced Short Palindromic Repeats ; Cyclin-Dependent Kinases/antagonists & inhibitors ; Epithelial Cells/physiology ; Female ; Gene Expression Regulation ; Gene Library ; Humans ; Mammary Glands, Animal ; Mice ; NF-kappa B/genetics ; NF-kappa B/metabolism ; Organoids/physiology ; Signal Transduction ; TNF Receptor-Associated Factor 3/genetics ; TNF Receptor-Associated Factor 3/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; NF-kappa B ; TNF Receptor-Associated Factor 3 ; Transcription Factors ; Yap1 protein, mouse ; tafazzin protein, mouse (EC 2.3.-) ; Cyclin-Dependent Kinases (EC 2.7.11.22)
Language	English
Publishing date	2020-11-13
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.63603
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Article ; Online: DNA Damage Promotes Epithelial Hyperplasia and Fate Mis-specification via Fibroblast Inflammasome Activation.

Seldin, Lindsey / Macara, Ian G

Developmental cell

2020 Volume 55, Issue 5, Page(s) 558–573.e6

Abstract: DNA crosslinking agents are commonly used in cancer chemotherapy; however, responses of normal tissues to these agents have not been widely investigated. We reveal in mouse interfollicular epidermal, mammary and hair follicle epithelia that genotoxicity ... ...

Abstract	DNA crosslinking agents are commonly used in cancer chemotherapy; however, responses of normal tissues to these agents have not been widely investigated. We reveal in mouse interfollicular epidermal, mammary and hair follicle epithelia that genotoxicity does not promote apoptosis but paradoxically induces hyperplasia and fate specification defects in quiescent stem cells. DNA damage to skin causes epithelial and dermal hyperplasia, tissue expansion, and proliferation-independent formation of abnormal K14/K10 dual-positive suprabasal cells. Unexpectedly, this behavior is epithelial cell non-autonomous and independent of an intact immune system. Instead, dermal fibroblasts are both necessary and sufficient to induce the epithelial response, which is mediated by activation of a fibroblast-specific NLRP3 inflammasome and subsequent IL-1β production. Thus, genotoxic agents that are used chemotherapeutically to promote cancer cell death can have the opposite effect on wild-type epithelia by inducing, via a non-autonomous IL-1β-driven mechanism, both hyperplasia and stem cell lineage defects.
MeSH term(s)	Animals ; Cell Plasticity/drug effects ; Cell Proliferation/drug effects ; DNA Damage ; Dermis/drug effects ; Dermis/pathology ; Epithelial Cells/drug effects ; Epithelial Cells/pathology ; Female ; Fibroblasts/drug effects ; Fibroblasts/pathology ; Hair Follicle/drug effects ; Hair Follicle/pathology ; Hyperplasia ; Inflammasomes/metabolism ; Interleukin-1beta/pharmacology ; Mammary Glands, Animal/drug effects ; Mammary Glands, Animal/pathology ; Mice ; Mutagens/toxicity ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Stem Cells/drug effects ; Stem Cells/metabolism
Chemical Substances	Inflammasomes ; Interleukin-1beta ; Mutagens ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nlrp3 protein, mouse
Language	English
Publishing date	2020-10-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2020.09.021
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Zs.A 5742: 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: Genome-wide CRISPR screen identifies noncanonical NF-κB signaling as a regulator of density-dependent proliferation

Maria Fomicheva / Ian G Macara

eLife, Vol

2020 Volume 9

Abstract	Epithelial cells possess intrinsic mechanisms to maintain an appropriate cell density for normal tissue morphogenesis and homeostasis. Defects in such mechanisms likely contribute to hyperplasia and cancer initiation. To identify genes that regulate the density-dependent proliferation of murine mammary epithelial cells, we developed a fluorescence-activated cell sorting assay based on fluorescence ubiquitination cell cycle indicator, which marks different stages of the cell cycle with distinct fluorophores. Using this powerful assay, we performed a genome-wide CRISPR/Cas9 knockout screen, selecting for cells that proliferate normally at low density but continue to divide at high density. Unexpectedly, one top hit was Traf3, a negative regulator of NF-κB signaling that has never previously been linked to density-dependent proliferation. We demonstrate that loss of Traf3 specifically activates noncanonical NF-κB signaling. This in turn triggers an innate immune response and drives cell division independently of known density-dependent proliferation mechanisms, including YAP/TAZ signaling and cyclin-dependent kinase inhibitors, by blocking entry into quiescence.
Keywords	homeostasis ; cell cycle ; epithelia ; innate immunity ; quiescence ; cancer ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2020-11-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The Par3 polarity protein is an exocyst receptor essential for mammary cell survival.

Ahmed, Syed Mukhtar / Macara, Ian G

Nature communications

2017 Volume 8, Page(s) 14867

Abstract: The exocyst is an essential component of the secretory pathway required for delivery of basolateral proteins to the plasma membranes of epithelial cells. Delivery occurs adjacent to tight junctions (TJ), suggesting that it recognizes a receptor at this ... ...

Abstract	The exocyst is an essential component of the secretory pathway required for delivery of basolateral proteins to the plasma membranes of epithelial cells. Delivery occurs adjacent to tight junctions (TJ), suggesting that it recognizes a receptor at this location. However, no such receptor has been identified. The Par3 polarity protein associates with TJs but has no known function in membrane traffic. We now show that, unexpectedly, Par3 is essential for mammary cell survival. Par3 silencing causes apoptosis, triggered by phosphoinositide trisphosphate depletion and decreased Akt phosphorylation, resulting from failure of the exocyst to deliver basolateral proteins to the cortex. A small region of PAR3 binds directly to Exo70 and is sufficient for exocyst docking, membrane-protein delivery and cell survival. PAR3 lacking this domain can associate with the cortex but cannot support exocyst function. We conclude that Par3 is the long-sought exocyst receptor required for targeted membrane-protein delivery.
MeSH term(s)	Animals ; Apoptosis ; Cadherins/metabolism ; Cell Adhesion Molecules/chemistry ; Cell Adhesion Molecules/deficiency ; Cell Adhesion Molecules/metabolism ; Cell Line ; Cell Polarity ; Cell Survival ; Enzyme Activation ; Epithelial Cells/metabolism ; Female ; Gene Knockdown Techniques ; Golgi Apparatus/metabolism ; Humans ; Lysine/metabolism ; Mammary Glands, Animal/cytology ; Models, Biological ; PTEN Phosphohydrolase/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Protein Domains ; Proto-Oncogene Proteins c-akt/metabolism ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Cadherins ; Cell Adhesion Molecules ; Pard3 protein, mouse ; Phosphatidylinositol Phosphates ; Vesicular Transport Proteins ; phosphatidylinositol 3,4,5-triphosphate ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; PTEN Phosphohydrolase (EC 3.1.3.67) ; rab11 protein (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2017-03-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms14867
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Article: Role of the Rab3A GTPase in regulated secretion from neuroendocrine cells.

Macara, I G

Trends in endocrinology and metabolism: TEM

2008 Volume 5, Issue 7, Page(s) 267–271

Abstract: Regulated secretion is a complex process that involves scores of distinct proteins. These proteins must assemble into machines that organize vesicle docking, membrane fusion, and recovery of vesicle components. Rab3A, a member of the Ras superfamily of ... ...

Abstract	Regulated secretion is a complex process that involves scores of distinct proteins. These proteins must assemble into machines that organize vesicle docking, membrane fusion, and recovery of vesicle components. Rab3A, a member of the Ras superfamily of GTPases, associates with secretory granule membranes of neuroendocrine cells, and mutants of Rab3A can inhibit exocytosis. A model is proposed in which Rab3A controls the assembly and disassembly of a docking complex that inhibits membrane fusion until an external signal triggers release of the Rab3A from the complex.
Language	English
Publishing date	2008-01-31
Publishing country	United States
Document type	Journal Article
ZDB-ID	1042384-9
ISSN	1879-3061 ; 1043-2760
ISSN (online)	1879-3061
ISSN	1043-2760
DOI	10.1016/1043-2760(94)p3201-h
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