ArticleThe Journal of biological chemistry2010
Phosphatidylinositol 4,5-bisphosphate activates Slo3 currents and its hydrolysis underlies the epidermal growth factor-induced current inhibition.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Discovery of non-opioid peptides that selectively relieve mechanical pain in rodents through inhibition of TRPV4 channels.Acta pharmacologica Sinica · 2026Article
- A synthetic peptide, derived from neurotoxin GsMTx4, acts as a non-opioid analgesic to alleviate mechanical and neuropathic pain through the TRPV4 channel.Acta pharmaceutica Sinica. B · 2025Article
- The sperm-specific KFrontiers in cell and developmental biology · 2024Article
- Spotlight on the Binding Affinity of Ion Channels for Phosphoinositides: From the Study of Sperm Flagellum.Frontiers in physiology · 2022Review
- Structure and Function of Ion Channels Regulating Sperm Motility-An Overview.International journal of molecular sciences · 2021Review
- Methods to study phosphoinositide regulation of ion channels.Methods in enzymology · 2021Article
- The Slo3/Lrrc52 complex is sensitive to phosphoinositides.Channels (Austin, Tex.) · 2020Article
- Polarized PtdIns(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The neuropeptide GsMTx4 inhibits a mechanosensitive BK channel through the voltage-dependent modification specific to mechano-gating.The Journal of biological chemistry · 2019Article
- Epilepsy-Related Slack Channel Mutants Lead to Channel Over-Activity by Two Different Mechanisms.Cell reports · 2016Article
- Mechanism of inhibition of mouse Slo3 (KCa 5.1) potassium channels by quinine, quinidine and barium.British journal of pharmacology · 2015Article
- Mutations in Nature Conferred a High Affinity Phosphatidylinositol 4,5-Bisphosphate-binding Site in Vertebrate Inwardly Rectifying Potassium Channels.The Journal of biological chemistry · 2015Article
- Structural analysis of dopamine- and amphetamine-induced depolarization currents in the human dopamine transporter.ACS chemical neuroscience · 2015Article
- Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels.Annual review of physiology · 2015Review
- Structural determinants of phosphatidylinositol 4,5-bisphosphate (PIP2) regulation of BK channel activity through the RCK1 Ca2+ coordination site.The Journal of biological chemistry · 2014Article
- K+ and Cl- channels and transporters in sperm function.Current topics in developmental biology · 2013Review
- Rediscovering sperm ion channels with the patch-clamp technique.Molecular human reproduction · 2011Review
- Ion channels, phosphorylation and mammalian sperm capacitation.Asian journal of andrology · 2011Review
- SLO-2 isoforms with unique Ca(2+) - and voltage-dependence characteristics confer sensitivity to hypoxia in C. elegans.Channels (Austin, Tex.)Article
- PIPThe Journal of biological chemistryArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The Slo3 gene encodes a high conductance potassium channel, which is activated by both voltage and intracellular alkalinization. Slo3 is specifically expressed in mammalian sperm cells, where it gives rise to pH-dependent outwardly rectifying K(+) currents. Sperm Slo3 is the main current responsible for the capacitation-induced hyperpolarization, which is required for the ensuing acrosome reaction, an exocytotic process essential for fertilization. Here we show that in intact spermatozoa and in a heterologous expression system, the activation of Slo3 currents is regulated by phosphatidylinositol 4,5-bisphosphate (PIP(2)). Depletion of endogenous PIP(2) in inside-out macropatches from Xenopus oocytes inhibited heterologously expressed Slo3 currents. Whole-cell recordings of sperm Slo3 currents or of Slo3 channels co-expressed in Xenopus oocytes with epidermal growth factor receptor, demonstrated that stimulation by epidermal growth factor (EGF) could inhibit channel activity in a PIP(2)-dependent manner. High concentrations of PIP(2) in the patch pipette not only resulted in a strong increase in sperm Slo3 current density but also prevented the EGF-induced inhibition of this current. Mutation of positively charged residues involved in channel-PIP(2) interactions enhanced the EGF-induced inhibition of Slo3 currents. Overall, our results suggest that PIP(2) is an important regulator for Slo3 activation and that receptor-mediated hydrolysis of PIP(2) leads to inhibition of Slo3 currents both in native and heterologous expression systems.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.