Electrophysiology of Concatameric Pannexin 1 Channels Reveals the Stoichiometry of C-Terminal Autoinhibition

Codi d'Art Públic: 8008-1 (La República); Reportatge realitzat als dies 4 i 18-7-1990Pericas, Enric (arquitecte); Viaplana, Albert (arquitecte i estructura); Viladomat Massanas, Josep (escultura);Joan Pie (Medalló); Piñón, Helio (Estr

Two-pore domain potassium channels (K2P) in GtoPdb v.2021.3

The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-forming α-subunit contains two pore loop (P) domains and two subunits assemble to form one ion conduction pathway lined by four P domains. It is important to note that single channels do not have two pores but that each subunit has two P domains in its primary sequence; hence the name two-pore domain, or K2P channels (and not two-pore channels). Some of the K2P subunits can form heterodimers across subfamilies (e.g. K2P3.1 with K2P9.1). The nomenclature of 4TM K channels in the literature is still a mixture of IUPHAR and common names. The suggested division into subfamilies, described in the More detailed introduction, is based on similarities in both structural and functional properties within subfamilies and this explains the "common abbreviation" nomenclature in the tables below

Two P domain potassium channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-forming α-subunit contains two pore loop (P) domains and two subunits assemble to form one ion conduction pathway lined by four P domains. It is important to note that single channels do not have two pores but that each subunit has two P domains in its primary sequence; hence the name two P domain, or K2P channels (and not two-pore channels). Some of the K2P subunits can form heterodimers across subfamilies (e.g. K2P3.1 with K2P9.1). The nomenclature of 4TM K channels in the literature is still a mixture of IUPHAR and common names. The suggested division into subfamilies, described in the More detailed introduction, is based on similarities in both structural and functional properties within subfamilies and this explains the "common abbreviation" nomenclature in the tables below

Two P domain potassium channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-forming α-subunit contains two pore loop (P) domains and two subunits assemble to form one ion conduction pathway lined by four P domains. It is important to note that single channels do not have two pores but that each subunit has two P domains in its primary sequence; hence the name two P domain, or K2P channels (and not two-pore channels). Some of the K2P subunits can form heterodimers across subfamilies (e.g. K2P3.1 with K2P9.1). The nomenclature of 4TM K channels in the literature is still a mixture of IUPHAR and common names. The suggested division into subfamilies, described in the More detailed introduction, is based on similarities in both structural and functional properties within subfamilies and this explains the "common abbreviation" nomenclature in the tables below

Two-pore domain potassium channels (K2P) in GtoPdb v.2023.1

The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-forming α-subunit contains two pore loop (P) domains and two subunits assemble to form one ion conduction pathway lined by four P domains. It is important to note that single channels do not have two pores but that each subunit has two P domains in its primary sequence; hence the name two-pore domain, or K2P channels (and not two-pore channels). Some of the K2P subunits can form heterodimers across subfamilies (e.g. K2P3.1 with K2P9.1). The nomenclature of 4TM K channels in the literature is still a mixture of IUPHAR and common names. The suggested division into subfamilies, described in the More detailed introduction, is based on similarities in both structural and functional properties within subfamilies and this explains the "common abbreviation" nomenclature in the tables below

Two P domain potassium channels in GtoPdb v.2021.2

The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-forming α-subunit contains two pore loop (P) domains and two subunits assemble to form one ion conduction pathway lined by four P domains. It is important to note that single channels do not have two pores but that each subunit has two P domains in its primary sequence; hence the name two P domain, or K2P channels (and not two-pore channels). Some of the K2P subunits can form heterodimers across subfamilies (e.g. K2P3.1 with K2P9.1). The nomenclature of 4TM K channels in the literature is still a mixture of IUPHAR and common names. The suggested division into subfamilies, described in the More detailed introduction, is based on similarities in both structural and functional properties within subfamilies and this explains the "common abbreviation" nomenclature in the tables below

Pannexin 1 channels facilitate communication between T cells to restrict the severity of airway inflammation

Allergic airway inflammation is driven by type-2 CD4(+) T cell inflammatory responses. We uncover an immunoregulatory role for the nucleotide release channel, Panx1, in T cell crosstalk during airway disease. Inverse correlations between Panx1 and asthmatics and our mouse models revealed the necessity, specificity, and sufficiency of Panx1 in T cells to restrict inflammation. Global Panx1(-/-) mice experienced exacerbated airway inflammation, and T-cell-specific deletion phenocopied Panx1(-/-) mice. A transgenic designed to re-express Panx1 in T cells reversed disease severity in global Panx1(-/-) mice. Panx1 activation occurred in pro-inflammatory T effector (Teff) and inhibitory T regulatory (Treg) cells and mediated the extracellular-nucleotide-based Treg-Teff crosstalk required for suppression of Teff cell proliferation. Mechanistic studies identified a Salt-inducible kinase-dependent phosphorylation of Panx1 serine 205 important for channel activation. A genetically targeted mouse expressing non-phosphorylatable Panx1S205A phenocopied the exacerbated inflammation in Panx1(-/-) mice. These data identify Panx1-dependent Treg:Teff cell communication in restricting airway disease

Early postnatal development of thyrotropin-releasing hormone (TRH) expression, TRH receptor binding, and TRH responses in neurons of rat brainstem

We investigated the postnatal development of the thyrotropin-releasing hormone (TRH)-containing raphe system in the brainstem of neonatal rats. Postnatal changes in TRH expression in nucleus (n.) raphe obscurus (ROb) and n. raphe pallidus (RPa) were evaluated by in situ hybridization using an 35S-labeled oligonucleotide probe complementary to TRH precursor mRNA. TRH mRNA expression was low at birth [postnatal day 0 (P0)], but was clearly evident by P7 and increased from that time to reach sustained high levels from P14 to P28. Consistent with this postnatal increase in TRH expression, we found increases in the density of TRH-immunoreactive (IR) fibers, which are derived from ROb and RPa, in the hypoglossal nucleus (nXII). TRH-IR fibers in nXII were very sparse at P0, but increased markedly over the first 2 postnatal weeks. The change in TRH innervation of nXII was closely matched by concomitant increases in 3H-methyl-TRH binding in nXII; specific TRH binding increased from very low levels at birth to high levels of P14. Finally, we recorded intracellularly the electrophysiological responses to TRH of hypoglossal motoneurons (HMs; n = 42) of neonatal rats (P0- P21) in a brainstem slice preparation. The response of neonatal HMs to TRH, in contrast to adult HMs, was highly variable. In some neonatal HMs, even at P0, TRH caused a depolarization with a decrease in input conductance (GN) that was characteristic of the response of all adult HMs. However, in other neonatal HMs, TRH was either without effect or caused a slight depolarization with no apparent change in GN, responses that were unlike those of adult HMs. A response was considered typical (i.e., “adult-like”) if GN decreased to < 85% of control. The percentage of cells responding in a typical manner increased progressively from 25% at P0-P2 to 100% after P11. In addition, we found that the density of TRH-sensitive current (normalized to cell capacitance) increased with postnatal age in HMs that responded in a typical manner, suggesting that expression of the TRH-sensitive conductance is also developmentally regulated. Together, these data indicate that the TRH raphe neuronal system of the rat brainstem is not fully mature at the time of birth but develops over the first few postnatal weeks. This was true of levels of TRH mRNA in caudal raphe nuclei, density of TRH-IR fibers and 3H-methyl-TRH binding in nXII, and also the manner and magnitude of electrophysiological responses of HMs to exogenously applied TRH