Literature DB >> 16533896

Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1.

Yuichiro Fujiwara1, Yoshihiro Kubo.   

Abstract

It is known that rectification of currents through the inward rectifier K(+) channel (Kir) is mainly due to blockade of the outward current by cytoplasmic Mg(2+) and polyamines. Analyses of the crystal structure of the cytoplasmic region of Kir2.1 have revealed the presence of both negatively (E224, D255, D259, and E299) and positively (R228 and R260) charged residues on the wall of the cytoplasmic pore of Kir2.1, but the detail is not known about the contribution of these charged residues, the positive charges in particular, to the inward rectification. We therefore analyzed the functional significance of these charged amino acids using single/double point mutants in order to better understand the structure-based mechanism underlying inward rectification of Kir2.1 currents. As a first step, we used two-electrode voltage clamp to examine inward rectification in systematically prepared mutants in which one or two negatively or positively charged amino acids were neutralized by substitution. We found that the intensity of the inward rectification tended to be determined by the net negative charge within the cytoplasmic pore. We then used inside-out excised patch clamp recording to analyze the effect of the mutations on blockade by intracellular blockers and on K(+) permeation. We observed that a decrease in the net negative charge within the cytoplasmic pore reduced both the susceptibility of the channel to blockade by Mg(2+) or spermine and the voltage dependence of the blockade. It also reduced K(+) permeation; i.e., it decreased single channel conductance, increased open-channel noise, and strengthened the intrinsic inward rectification in the total absence of cytoplasmic blockers. Taken together, these data suggest that the negatively charged cytoplasmic pore of Kir electrostatically gathers cations such as Mg(2+), spermine, and K(+) so that the transmembrane pore is sufficiently filled with K(+) ions, which enables strong voltage-dependent blockade with adequate outward K(+) conductance.

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Year:  2006        PMID: 16533896      PMCID: PMC2151513          DOI: 10.1085/jgp.200509434

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  58 in total

1.  Role of ER export signals in controlling surface potassium channel numbers.

Authors:  D Ma; N Zerangue; Y F Lin; A Collins; M Yu; Y N Jan; L Y Jan
Journal:  Science       Date:  2001-01-12       Impact factor: 47.728

2.  Mechanism of IRK1 channel block by intracellular polyamines.

Authors:  D Guo; Z Lu
Journal:  J Gen Physiol       Date:  2000-06       Impact factor: 4.086

3.  Cloning and expression of an inwardly rectifying ATP-regulated potassium channel.

Authors:  K Ho; C G Nichols; W J Lederer; J Lytton; P M Vassilev; M V Kanazirska; S C Hebert
Journal:  Nature       Date:  1993-03-04       Impact factor: 49.962

4.  Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel.

Authors:  Y Kubo; E Reuveny; P A Slesinger; Y N Jan; L Y Jan
Journal:  Nature       Date:  1993-08-26       Impact factor: 49.962

5.  Electrostatic tuning of Mg2+ affinity in an inward-rectifier K+ channel.

Authors:  Z Lu; R MacKinnon
Journal:  Nature       Date:  1994-09-15       Impact factor: 49.962

6.  Gating of inwardly rectifying K+ channels localized to a single negatively charged residue.

Authors:  B A Wible; M Taglialatela; E Ficker; A M Brown
Journal:  Nature       Date:  1994-09-15       Impact factor: 49.962

7.  Control of rectification and permeation by two distinct sites after the second transmembrane region in Kir2.1 K+ channel.

Authors:  Y Kubo; Y Murata
Journal:  J Physiol       Date:  2001-03-15       Impact factor: 5.182

8.  Architecture of a K+ channel inner pore revealed by stoichiometric covalent modification.

Authors:  T Lu; B Nguyen; X Zhang; J Yang
Journal:  Neuron       Date:  1999-03       Impact factor: 17.173

9.  A dynamic model of the cardiac ventricular action potential. I. Simulations of ionic currents and concentration changes.

Authors:  C H Luo; Y Rudy
Journal:  Circ Res       Date:  1994-06       Impact factor: 17.367

10.  Pore block versus intrinsic gating in the mechanism of inward rectification in strongly rectifying IRK1 channels.

Authors:  D Guo; Z Lu
Journal:  J Gen Physiol       Date:  2000-10       Impact factor: 4.086

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  32 in total

1.  Charges in the cytoplasmic pore control intrinsic inward rectification and single-channel properties in Kir1.1 and Kir2.1 channels.

Authors:  Hsueh-Kai Chang; Shih-Hao Yeh; Ru-Chi Shieh
Journal:  J Membr Biol       Date:  2007-06-14       Impact factor: 1.843

2.  The bundle crossing region is responsible for the inwardly rectifying internal spermine block of the Kir2.1 channel.

Authors:  Chiung-Wei Huang; Chung-Chin Kuo
Journal:  Pflugers Arch       Date:  2013-07-20       Impact factor: 3.657

3.  Polyamine block of inwardly rectifying potassium channels.

Authors:  Harley T Kurata; Wayland W L Cheng; Colin G Nichols
Journal:  Methods Mol Biol       Date:  2011

4.  Multi-ion versus single-ion conduction mechanisms can yield current rectification in biological ion channels.

Authors:  Tamsyn A Hilder; Ben Corry; Shin-Ho Chung
Journal:  J Biol Phys       Date:  2014-01-26       Impact factor: 1.365

5.  The anti-protozoal drug pentamidine blocks KIR2.x-mediated inward rectifier current by entering the cytoplasmic pore region of the channel.

Authors:  T P de Boer; L Nalos; A Stary; B Kok; M J C Houtman; G Antoons; T A B van Veen; J D M Beekman; B L de Groot; T Opthof; M B Rook; M A Vos; M A G van der Heyden
Journal:  Br J Pharmacol       Date:  2010-02-24       Impact factor: 8.739

6.  Caffeine activates mouse TRPA1 channels but suppresses human TRPA1 channels.

Authors:  Katsuhiro Nagatomo; Yoshihiro Kubo
Journal:  Proc Natl Acad Sci U S A       Date:  2008-11-06       Impact factor: 11.205

7.  Locale and chemistry of spermine binding in the archetypal inward rectifier Kir2.1.

Authors:  Harley T Kurata; Emily A Zhu; Colin G Nichols
Journal:  J Gen Physiol       Date:  2010-05       Impact factor: 4.086

8.  Evidence for the direct interaction of spermine with the inwardly rectifying potassium channel.

Authors:  Masanori Osawa; Mariko Yokogawa; Takahiro Muramatsu; Tomomi Kimura; Yoko Mase; Ichio Shimada
Journal:  J Biol Chem       Date:  2009-07-20       Impact factor: 5.157

9.  The molecular basis of chloroquine block of the inward rectifier Kir2.1 channel.

Authors:  Aldo A Rodríguez-Menchaca; Ricardo A Navarro-Polanco; Tania Ferrer-Villada; Jason Rupp; Frank B Sachse; Martin Tristani-Firouzi; José A Sánchez-Chapula
Journal:  Proc Natl Acad Sci U S A       Date:  2008-01-23       Impact factor: 11.205

10.  Saturation and microsecond gating of current indicate depletion-induced instability of the MaxiK selectivity filter.

Authors:  Indra Schroeder; Ulf-Peter Hansen
Journal:  J Gen Physiol       Date:  2007-07       Impact factor: 4.086

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