FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2897538931> ?p ?o ?g. }

• W2897538931 endingPage "18802" @default.
• W2897538931 startingPage "18789" @default.
• W2897538931 abstract "Most excitatory neurotransmission in the mammalian brain is mediated by a family of plasma membrane–bound signaling proteins called ionotropic glutamate receptors (iGluRs). iGluRs assemble at central synapses as tetramers, forming a central ion-channel pore whose primary function is to rapidly transport Na+ and Ca2+ in response to binding the neurotransmitter l-glutamic acid. The pore of iGluRs is also accessible to bulkier cytoplasmic cations, such as the polyamines spermine, spermidine, and putrescine, which are drawn into the permeation pathway, but get stuck and block the movement of other ions. The degree of this polyamine-mediated channel block is highly regulated by processes that control the free cytoplasmic polyamine concentration, the membrane potential, or the iGluR subunit composition. Recently, an additional regulation by auxiliary proteins, most notably transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory proteins (TARPs), cornichons, and neuropilin and tolloid-like proteins (NETOs), has been identified. Here, I review what we have learned of polyamine block of iGluRs and its regulation by auxiliary subunits. TARPs, cornichons, and NETOs attenuate the channel block by enabling polyamines to exit the pore. As a result, polyamine permeation occurs at more negative and physiologically relevant membrane potentials. The structural basis for enhanced polyamine transport remains unresolved, although alterations in both channel architecture and charge-screening mechanisms have been proposed. That auxiliary subunits can attenuate the polyamine block reveals an unappreciated impact of polyamine permeation in shaping the signaling properties of neuronal AMPA- and kainate-type iGluRs. Moreover, enhanced polyamine transport through iGluRs may have a role in regulating cellular polyamine levels. Most excitatory neurotransmission in the mammalian brain is mediated by a family of plasma membrane–bound signaling proteins called ionotropic glutamate receptors (iGluRs). iGluRs assemble at central synapses as tetramers, forming a central ion-channel pore whose primary function is to rapidly transport Na+ and Ca2+ in response to binding the neurotransmitter l-glutamic acid. The pore of iGluRs is also accessible to bulkier cytoplasmic cations, such as the polyamines spermine, spermidine, and putrescine, which are drawn into the permeation pathway, but get stuck and block the movement of other ions. The degree of this polyamine-mediated channel block is highly regulated by processes that control the free cytoplasmic polyamine concentration, the membrane potential, or the iGluR subunit composition. Recently, an additional regulation by auxiliary proteins, most notably transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory proteins (TARPs), cornichons, and neuropilin and tolloid-like proteins (NETOs), has been identified. Here, I review what we have learned of polyamine block of iGluRs and its regulation by auxiliary subunits. TARPs, cornichons, and NETOs attenuate the channel block by enabling polyamines to exit the pore. As a result, polyamine permeation occurs at more negative and physiologically relevant membrane potentials. The structural basis for enhanced polyamine transport remains unresolved, although alterations in both channel architecture and charge-screening mechanisms have been proposed. That auxiliary subunits can attenuate the polyamine block reveals an unappreciated impact of polyamine permeation in shaping the signaling properties of neuronal AMPA- and kainate-type iGluRs. Moreover, enhanced polyamine transport through iGluRs may have a role in regulating cellular polyamine levels." @default.
• W2897538931 created "2018-10-26" @default.
• W2897538931 creator A5008112491 @default.
• W2897538931 date "2018-11-01" @default.
• W2897538931 modified "2023-09-27" @default.
• W2897538931 title "Polyamine-mediated channel block of ionotropic glutamate receptors and its regulation by auxiliary proteins" @default.
• W2897538931 cites W1000930439 @default.
• W2897538931 cites W1209483732 @default.
• W2897538931 cites W1483803603 @default.
• W2897538931 cites W1485031809 @default.
• W2897538931 cites W1489400020 @default.
• W2897538931 cites W1509552674 @default.
• W2897538931 cites W1513950254 @default.
• W2897538931 cites W1518638243 @default.
• W2897538931 cites W1520077268 @default.
• W2897538931 cites W1538207507 @default.
• W2897538931 cites W1543054176 @default.
• W2897538931 cites W1544008935 @default.
• W2897538931 cites W1548733397 @default.
• W2897538931 cites W1549420856 @default.
• W2897538931 cites W1557041093 @default.
• W2897538931 cites W1567416559 @default.
• W2897538931 cites W1568697641 @default.
• W2897538931 cites W1585464522 @default.
• W2897538931 cites W1658796519 @default.
• W2897538931 cites W1810179799 @default.
• W2897538931 cites W1827988151 @default.
• W2897538931 cites W1867012516 @default.
• W2897538931 cites W1885859263 @default.
• W2897538931 cites W1963786372 @default.
• W2897538931 cites W1966669109 @default.
• W2897538931 cites W1967209558 @default.
• W2897538931 cites W1969942127 @default.
• W2897538931 cites W1971347175 @default.
• W2897538931 cites W1971372933 @default.
• W2897538931 cites W1972391943 @default.
• W2897538931 cites W1973796039 @default.
• W2897538931 cites W1974424738 @default.
• W2897538931 cites W1975419967 @default.
• W2897538931 cites W1983071240 @default.
• W2897538931 cites W1984117397 @default.
• W2897538931 cites W1984660568 @default.
• W2897538931 cites W1984804294 @default.
• W2897538931 cites W1984880167 @default.
• W2897538931 cites W1988427300 @default.
• W2897538931 cites W1988958893 @default.
• W2897538931 cites W1993536619 @default.
• W2897538931 cites W1993782794 @default.
• W2897538931 cites W1996208391 @default.
• W2897538931 cites W1996712322 @default.
• W2897538931 cites W1999107947 @default.
• W2897538931 cites W1999968276 @default.
• W2897538931 cites W2000300989 @default.
• W2897538931 cites W2001795351 @default.
• W2897538931 cites W2002938146 @default.
• W2897538931 cites W2004277471 @default.
• W2897538931 cites W2004643793 @default.
• W2897538931 cites W2005807247 @default.
• W2897538931 cites W2008283517 @default.
• W2897538931 cites W2010930826 @default.
• W2897538931 cites W2011244895 @default.
• W2897538931 cites W2011545647 @default.
• W2897538931 cites W2011587060 @default.
• W2897538931 cites W2011630286 @default.
• W2897538931 cites W2012678641 @default.
• W2897538931 cites W2014765513 @default.
• W2897538931 cites W2017472306 @default.
• W2897538931 cites W2017506356 @default.
• W2897538931 cites W2020931572 @default.
• W2897538931 cites W2023130009 @default.
• W2897538931 cites W2023944340 @default.
• W2897538931 cites W2024763972 @default.
• W2897538931 cites W2025994995 @default.
• W2897538931 cites W2026872153 @default.
• W2897538931 cites W2027046812 @default.
• W2897538931 cites W2028953339 @default.
• W2897538931 cites W2029508498 @default.
• W2897538931 cites W2031074940 @default.
• W2897538931 cites W2031328241 @default.
• W2897538931 cites W2034009493 @default.
• W2897538931 cites W2036313253 @default.
• W2897538931 cites W2037852973 @default.
• W2897538931 cites W2039906334 @default.
• W2897538931 cites W2040091117 @default.
• W2897538931 cites W2040553608 @default.
• W2897538931 cites W2042678699 @default.
• W2897538931 cites W2043874825 @default.
• W2897538931 cites W2045674449 @default.
• W2897538931 cites W2046641567 @default.
• W2897538931 cites W2047688116 @default.
• W2897538931 cites W2047835829 @default.
• W2897538931 cites W2051084778 @default.
• W2897538931 cites W2052000300 @default.
• W2897538931 cites W2052960183 @default.
• W2897538931 cites W2053303814 @default.
• W2897538931 cites W2053739294 @default.
• W2897538931 cites W2055252729 @default.
• W2897538931 cites W2056025481 @default.

• next