SPRY3

Last update 08 May 2025

Basic Info

Synonyms

HSPRY3, Protein sprouty homolog 3, sprouty RTK signaling antagonist 3

+ [3]

Introduction

Inhibits neurite branching, arbor length and neurite complexity (By similarity). Inhibits EGF-mediated p42/44 ERK signaling (By similarity). Negatively regulates the MAPK cascade, resulting in a reduction of extracellular matrix protein accumulation (PubMed:30878395). May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis (PubMed:9458049).

100 Clinical Results associated with SPRY3

100 Translational Medicine associated with SPRY3

0 Patents (Medical) associated with SPRY3

Literatures (Medical) associated with SPRY3

01 Jun 2025·Non-coding RNA Research

Lnc-RAINY regulates genes involved in radiation susceptibility through DNA:DNA:RNA triplex-forming interactions and has tumor therapeutic potential in lung cancers

Article

Author: Patel, Kiran J ; Westemeier-Rice, Emily S ; Rawson, Travis W ; McLaughlin, Sarah ; Dziadowicz, Sebastian ; Martinez, Ivan ; McHugh, Olivia ; Ward, Sierra ; Misra, Bishal ; Winters, Michael T ; Yi, Weijun ; Hu, Gangqing ; Stewart, Amanda ; Bobbala, Sharan

Lung cancer is the leading cause of cancer related deaths worldwide. Unfortunately, radiation resistance remains a major problem facing lung cancer patients. Recently, we identified a group of long non-coding RNAs (lncRNAs) known as linc-SPRY3 RNAs, expressed on the Y-chromosome, which play a role in radiation sensitivity by decreasing tumor burden in vitro and in vivo after radiation. In this study, we found that the linc-SPRY3 RNAs are one large lncRNA that we named Radiation Induced Y-chromosome linked long non-coding RNA (lnc-RAINY). Through ATAC-seq and immunoprecipitation experiments, we show that lnc-RAINY interacts with DNA in a triple helix to induce chromatin remodeling and gene expression. We also identified that lnc-RAINY regulates CDC6 and CDC25A expression affecting senescence induction, cell migration patterns, and cell cycle regulation. Furthermore, the administration of Lnc-RAINY encapsulated in FDA-approved nanoparticles into a lung cancer patient-derived xenograft model dramatically reduces tumor progression demonstrating therapeutic potential.

01 Jun 2024·Stem Cell Research

Generation of two iPSC lines from adult central core disease patients with dominant missense variants in the RYR1 gene

Article

Author: Larmonier, Thierry ; Vo, Christina ; Scriba, Carolin K ; Clayton, Joshua S ; Saker, Safaa ; Ravenscroft, Gianina ; Malfatti, Edoardo ; Crane, Jordan ; Romero, Norma B ; Laing, Nigel G ; Taylor, Rhonda L

RYR1 variants are a common cause of congenital myopathies, including multi-minicore disease (MmD) and central core disease (CCD). Here, we generated iPSC lines from two CCD patients with dominant RYR1 missense variants that affect the transmembrane (pore) and SPRY3 protein domains (p.His4813Tyr and p.Asn1346Lys, respectively). Both lines had typical iPSC morphology, expressed canonical pluripotency markers, exhibited trilineage differentiation potential, and had normal karyotypes. Together with existing RYR1 iPSC lines, these represent important tools to study and develop treatments for RYR1-related myopathies.

20 Oct 2023·ACS Chemical Biology

RyR2 Binding of an Antiarrhythmic Cyclic Depsipeptide Mapped Using Confocal Fluorescence Lifetime Detection of FRET

Article

Author: Šeflová, Jaroslava ; Svensson, Bengt ; Blackwell, Daniel J. ; Johnston, Jeffrey N. ; Schwarz, Jacob A. ; Smith, Abigail N. ; Phillips, Taylor A. ; Knollmann, Björn C. ; Robia, Seth L. ; Thomas, David D. ; Rebbeck, Robyn T. ; Bovo, Elisa ; Van Petegem, Filip ; Nikolaienko, Roman ; Cornea, Răzvan L. ; Zima, Aleksey V.

Hyperactivity of cardiac sarcoplasmic reticulum (SR) ryanodine receptor (RyR2) Ca²⁺-release channels contributes to heart failure and arrhythmias. Reducing the RyR2 activity, particularly during cardiac relaxation (diastole), is a desirable therapeutic goal. We previously reported that the unnatural enantiomer (ent) of an insect-RyR activator, verticilide, inhibits porcine and mouse RyR2 at diastolic (nanomolar) Ca²⁺ and has in vivo efficacy against atrial and ventricular arrhythmia. To determine the ent-verticilide structural mode of action on RyR2 and guide its further development via medicinal chemistry structure-activity relationship studies, here, we used fluorescence lifetime (FLT)-measurements of Förster resonance energy transfer (FRET) in HEK293 cells expressing human RyR2. For these studies, we used an RyR-specific FRET molecular-toolkit and computational methods for trilateration (i.e., using distances to locate a point of interest). Multiexponential analysis of FLT-FRET measurements between four donor-labeled FKBP12.6 variants and acceptor-labeled ent-verticilide yielded distance relationships placing the acceptor probe at two candidate loci within the RyR2 cryo-EM map. One locus is within the Ry12 domain (at the corner periphery of the RyR2 tetrameric complex). The other locus is sandwiched at the interface between helical domain 1 and the SPRY3 domain. These findings document RyR2-target engagement by ent-verticilide, reveal new insight into the mechanism of action of this new class of RyR2-targeting drug candidate, and can serve as input in future computational determinations of the ent-verticilide binding site on RyR2 that will inform structure-activity studies for lead optimization.

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SPRY3

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