0000000000486266

AUTHOR

Deva Krupakar Kusuluri

showing 4 related works from this author

RPGR protein complex regulates proteasome activity and mediates store-operated calcium entry

2018

Ciliopathies are a group of genetically heterogeneous disorders, characterized by defects in cilia genesis or maintenance. Mutations in the RPGR gene and its interacting partners, RPGRIP1 and RPGRIP1L, cause ciliopathies, but the function of their proteins remains unclear. Here we show that knockdown (KD) of RPGR, RPGRIP1 or RPGRIP1L in hTERT-RPE1 cells results in abnormal actin cytoskeleton organization. The actin cytoskeleton rearrangement is regulated by the small GTPase RhoA via the planar cell polarity (PCP) pathway. RhoA activity was upregulated in the absence of RPGR, RPGRIP1 or RPGRIP1L proteins. In RPGR, RPGRIP1 or RPGRIP1L KD cells, we observed increased levels of DVl2 and DVl3 pr…

0301 basic medicineRMRHOAactin cytoskeletonbiologyChemistryEndoplasmic reticulumCiliumSTIM1RPGR complex030105 genetics & heredityActin cytoskeletonStore-operated calcium entryActin cytoskeleton organizationeye diseasesCell biology03 medical and health sciencesendoplasmic reticulum030104 developmental biologyciliopathyOncologybiology.proteinSmall GTPasestore-operated Ca2+ entryResearch PaperOncotarget
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Identification of Protein Complexes Associated with the Usher Syndrome 2C and Epilepsy-Associated Protein VLGR1 Applying Affinity Proteomics

2017

Authors aimed to identify novel VLGR1-associated protein networks to shed light on its integration into signaling pathways and the cellular compartments in which VLGR1 functions using high-resolution affinity proteomics based on tandem affinity purifications (TAPs).

0301 basic medicineChemistryUsher syndromeGenomics02 engineering and technologyComputational biology021001 nanoscience & nanotechnologymedicine.diseaseProteomics03 medical and health sciencesEpilepsy030104 developmental biologymedicineIdentification (biology)Signal transduction0210 nano-technologyProtein networkCellular compartmentGenomics and Computational Biology
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The expanding functional roles and signaling mechanisms of adhesion G protein-coupled receptors.

2019

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 (7TM) domain via a GPCR-autoproteolysis inducing (GAIN) domain containing a GPCR proteolytic site (GPS). Most aGPCRs undergo autoproteolysis at the GPS motif, but the cleaved fragments stay closely associated, with the N-terminal fragment (NTF) bound to the 7TM of the C-terminal fragment (CTF). The NTFs of most aGPCRs contain domains known to be involved in cell-cell adhesion, while the CTFs are involved in classical G protein signaling, as well…

0301 basic medicineG proteinGeneral Science & TechnologyArticleGeneral Biochemistry Genetics and Molecular BiologyReceptors G-Protein-Coupledimmunology03 medical and health sciencesG-Protein-Coupled0302 clinical medicineHistory and Philosophy of ScienceReceptorsExtracellularAnimalsHumanscancerstructural biologymechanosensationReceptordevelopmentG protein-coupled receptorChemistryGeneral NeuroscienceneurobiologySciences bio-médicales et agricolesTransmembrane proteinCell biology030104 developmental biologyStructural biologyGeneric health relevanceSignal transductionadhesion G protein-coupled receptor030217 neurology & neurosurgeryIntracellularsignal transductionSignal Transduction
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Adhesion G protein-coupled receptor VLGR1/ADGRV1 regulates cell spreading and migration by mechanosensing at focal adhesions.

2021

Summary VLGR1 (very large G protein-coupled receptor-1) is by far the largest adhesion G protein-coupled receptor in humans. Homozygous pathologic variants of VLGR1 cause hereditary deaf blindness in Usher syndrome 2C and haploinsufficiency of VLGR1 is associated with epilepsy. However, its molecular function remains elusive. Herein, we used affinity proteomics to identify many components of focal adhesions (FAs) in the VLGR1 interactome. VLGR1 is localized in FAs and assembles in FA protein complexes in situ. Depletion or loss of VLGR1 decreases the number and length of FAs in hTERT-RPE1 cells and in astrocytes of Vlgr1 mutant mice. VLGR1 depletion reduces cell spread and migration kinetic…

0301 basic medicineBiomoleculesMultidisciplinaryChemistryScienceQCell02 engineering and technologyCell Biology021001 nanoscience & nanotechnologyProteomicsInteractomeArticleCell biologyFocal adhesion03 medical and health sciences030104 developmental biologyMetabotropic receptormedicine.anatomical_structuremedicine0210 nano-technologyHaploinsufficiencyReceptorMolecular BiologyG protein-coupled receptoriScience
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