Výsledky vyhledávání - "Angeline M. Lyon"

Functional and structural characterization of allosteric activation of phospholipase Cε by Rap1A

Autor: Angeline M. Lyon, Elisabeth E. Garland-Kuntz, Monita Sieng, Andrea T. Marti, Arielle F. Selvia, Isaac J. Fisher, Jesse B. Hopkins

Publikováno v: The Journal of Biological Chemistry

Phospholipase Ce (PLCe) is activated downstream of G protein–coupled receptors and receptor tyrosine kinases through direct interactions with small GTPases, including Rap1A and Ras. Although Ras has been reported to allosterically activate the lipa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85f33d54d16b1d73f74df35a33fb24f6
http://europepmc.org/articles/PMC7864056

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Structure of phospholipase Cε reveals an integrated RA1 domain and previously unidentified regulatory elements

Autor: William Mbongo, Ngango Y Rugema, Amanda Everly, Kaushik Muralidharan, Angeline M. Lyon, Emmanda McKenzie, Hannah O'Neill, Elisabeth E. Garland-Kuntz, Andrea T. Marti, Monita Sieng, Arielle F. Selvia, Michelle M. Van Camp

Publikováno v: Communications Biology, Vol 3, Iss 1, Pp 1-10 (2020)
Communications Biology

Phospholipase Cε (PLCε) generates lipid-derived second messengers at the plasma and perinuclear membranes in the cardiovascular system. It is activated in response to a wide variety of signals, such as those conveyed by Rap1A and Ras, through a mec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::761a090c6c71832fbc27e264e710f832
http://link.springer.com/article/10.1038/s42003-020-01178-8

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Gαq and the Phospholipase Cβ3 X–Y Linker Regulate Adsorption and Activity on Compressed Lipid Monolayers

Autor: Keshav K. Prahalad, Rachel E. Jessup, Brianna N. Hudson, Angeline M. Lyon

Publikováno v: Biochemistry. 58:3454-3467

Phospholipase Cβ (PLCβ) enzymes are peripheral membrane proteins required for normal cardiovascular function. PLCβ hydrolyzes phosphatidylinositol 4,5-bisphosphate, producing second messengers that...

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cfeeedaf42cb167bed819c615f118abd
https://doi.org/10.1021/acs.biochem.9b00441

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High-resolution structure of RGS17 suggests a role for Ca2+ in promoting the GTPase-activating protein activity by RZ subfamily members

Autor: David L. Roman, Joseph B. O’Brien, C. Andrew Fowler, Jon C. D. Houtman, Michael P. Hayes, Angeline M. Lyon, Monita Sieng

Publikováno v: Journal of Biological Chemistry. 294:8148-8160

Regulator of G protein signaling (RGS) proteins are negative regulators of G protein–coupled receptor (GPCR) signaling through their ability to act as GTPase-activating proteins (GAPs) for activated Gα subunits. Members of the RZ subfamily of RGS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0b8c5e9632e85228a3990f2831928336
https://doi.org/10.1074/jbc.ra118.006059

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Functional and structural characterization of allosteric activation of Phospholipase Cε by Rap1A

Autor: Elisabeth E. Garland-Kuntz, Monita Sieng, Arielle F. Selvia, Jesse B. Hopkins, Isaac J. Fisher, Angeline M. Lyon, Andrea T. Marti

Phospholipase Cε (PLCε) is activated downstream of G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) through direct interactions with small GTPases, including Rap1A and Ras. While Ras has been reported to allosterically activ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4c080a97aac5aaa964fb884253c3b3f8
https://doi.org/10.1101/2020.07.10.191643

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Direct observation of conformational dynamics of the PH domain in phospholipases Cɛ and β may contribute to subfamily-specific roles in regulation

Autor: Arryn T. Blaine, Michelle Van Camp, Srinivas Chakravarthy, Wen Jiang, Frank S. Vago, Elisabeth E. Garland-Kuntz, Clairissa Corpstein, Monita Sieng, Angeline M. Lyon

Publikováno v: Journal of Biological Chemistry. 293:17477-17490

Phospholipase C (PLC) enzymes produce second messengers that increase the intracellular Ca(2+) concentration and activate protein kinase C (PKC). These enzymes also share a highly conserved arrangement of core domains. However, the contributions of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d698c7c08011db6150fd9591ebcfbda
https://doi.org/10.1074/jbc.ra118.003656

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Phospholipase Cβ3 Membrane Adsorption and Activation Are Regulated by Its C-Terminal Domains and Phosphatidylinositol 4,5-Bisphosphate

Autor: David H. Thompson, Seok-Hee Hyun, Brianna N. Hudson, Angeline M. Lyon

Publikováno v: Biochemistry. 56:5604-5614

Phospholipase Cβ (PLCβ) enzymes hydrolyze phosphatidylinositol 4,5-bisphosphate to produce second messengers that regulate intracellular Ca2+, cell proliferation, and survival. Their activity is dependent upon interfacial activation that occurs upo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37883b74ff4634069b048e79421d7097
https://doi.org/10.1021/acs.biochem.7b00547

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