A new human NHERF1 mutation decreases renal phosphate transporter NPT2a expression by a PTH-independent mechanism.

Autor: Marie Courbebaisse, Christine Leroy, Naziha Bakouh, Christine Salaün, Laurent Beck, Bernard Grandchamp, Gabrielle Planelles, Randy A Hall, Gérard Friedlander, Dominique Prié

Publikováno v: PLoS ONE, Vol 7, Iss 4, p e34764 (2012)

BackgroundThe sodium-hydrogen exchanger regulatory factor 1 (NHERF1) binds to the main renal phosphate transporter NPT2a and to the parathyroid hormone (PTH) receptor. We have recently identified mutations in NHERF1 that decrease renal phosphate reab

Externí odkaz: https://doaj.org/article/0255d0a5a6ce4c6c89a90858da2ad581

Phosphatidylserine exposure modulates adhesion GPCR BAI1 (ADGRB1) signaling activity

Autor: Trisha Lala, Juleva K. Doan, Hiroyuki Takatsu, H. Criss Hartzell, Hye-Won Shin, Randy A. Hall

Publikováno v: Journal of Biological Chemistry. 298:102685

Brain-specific angiogenesis inhibitor 1 (BAI1; also called ADGRB1 or B1) is an adhesion G protein-coupled receptor known from studies on macrophages to bind to phosphatidylserine (PS) on apoptotic cells via its N-terminal thrombospondin repeats. A se

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf8e75a5e95fb0c38764fdef5edf9d2
https://doi.org/10.1016/j.jbc.2022.102685

Mice lacking full length Adgrb1 (Bai1) exhibit social deficits, increased seizure susceptibility, and altered brain development

Autor: Fu Hung Shiu, Jennifer C. Wong, Takahiro Yamamoto, Trisha Lala, Ryan H. Purcell, Sharon Owino, Dan Zhu, Erwin G. Van Meir, Randy A. Hall, Andrew Escayg

Publikováno v: Exp Neurol

The adhesion G protein-coupled receptor BAI1/ADGRB1 plays an important role in suppressing angiogenesis, mediating phagocytosis, and acting as a brain tumor suppressor. BAI1 is also a critical regulator of dendritic spine and excitatory synapse devel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2afa399d29861f947d4900e1faa68822
https://doi.org/10.1016/j.expneurol.2022.113994

A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases receptor signaling activity

Autor: Ryan H. Purcell, William A. Gahl, Camilo Toro, Randy A. Hall

Publikováno v: Human Mutation. 38:1751-1760

Mutations in G protein-coupled receptors (GPCRs) that increase constitutive signaling activity can cause human disease. A de novo C-terminal mutation (R1465W) in the adhesion GPCR BAI2 (also known as ADGRB2) was identified in a patient suffering from

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b82ffae21a08e06b8905b3a5db7c1628
https://doi.org/10.1002/humu.23336

The expanding functional roles and signaling mechanisms of adhesion G protein-coupled receptors

Autor: Simone Prömel, Swati Srivastava, Nariman Balenga, Demet Araç, Hee Yong Kim, Nicole Scholz, Uwe Wolfrum, Yuri A. Ushkaryov, Rory K. Morgan, Randy A. Hall, Mario Vallon, James P. Bridges, Deva Krupakar Kusuluri, Gabriela Aust, Benoit Vanhollebeke, Ryan S. Gray, Antony A. Boucard, Xianhua Piao, Kelly R. Monk, Katherine Leon, Amit Mogha, Erwin G. Van Meir, Maike D. Glitsch, Cheng-Chih Hsiao, Kevin M. Wright, Ines Liebscher, Garret R. Anderson, Alexander Bernd Knierim, Caroline J. Formstone, Felix B. Engel, Kimberley F. Tolias, Doreen Thor

Publikováno v: Annals of the New York Academy of Sciences, vol 1456, iss 1
Annals of the New York Academy of Sciences, 1456(1), 5-25. Wiley-Blackwell
Ann N Y Acad Sci
Annals of the New York Academy of Sciences

The adhesion class of G protein-coupled receptors (GPCRs) is the second largest family of GPCRs (33 members in humans). Adhesion GPCRs (aGPCRs) are defined by a large extracellular N-terminal region that is linked to a C-terminal seven transmembrane

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13a5f5f51f91694384a721cf3709b948
https://escholarship.org/uc/item/9j92p473