Correction: Glutamate transporters: A broad review of the most recent archaeal and human structures

TY - JOUR

T1 - Correction

T2 - Glutamate transporters: A broad review of the most recent archaeal and human structures

AU - Pavić, Ana

AU - Holmes, Alexandra O.M.

AU - Postis, Vincent L.G.

AU - Goldman, Adrian

N1 - Publisher Copyright: © 2019 The Author(s).

PY - 2019/9/5

Y1 - 2019/9/5

N2 - It has come to the attention of the authors that a citation for Figure 4 was omitted from the caption. The caption should read: Figure 4. Predicted anion permeation pathway. A GltPh monomer viewed from the trimerization interface. The residues R276 and M395 responsible for the anion selectivity are indicated. The orange circles represent 'snapshots' of the path of a chloride ion through the channel between the two domains. Part of the scaffold domain has been removed for clarity. Figure adapted from [49]. Additionally, some references were incorrectly cited in the second paragraph of the section 'Uncoupled Chloride Conductance'. The paragraph should read: Initially, chloride permeation was proposed to occur along TM2 [47]. The Ser to Val mutation on TM2 (residue 65 in GltPh and 103 in EAAT1) strongly affected chloride permeation [8,47]. The GltPh structure in an intermediate OFC suggested that there was an aqueous cavity that might serve as a permeation pathway for anions [14]. Subsequent research has suggested that substrate transport and anion permeation proceed through two mutually exclusive pathways separated by a flexible wall domain and facilitated by the conformational changes [48,49]. The moving flexible wall is composed of several residues in HP1, HP2 hairpins and TM8 (Figure 4), the movement of which dictate the pathway [49]. Arg276 in HP1 and Met395, predicted to line the anion pore [49], were shown to exhibit a significant Cl-selectivity over Na+ in both simulations and experiments: Anion selectivity is impaired by the insertion of negatively charged side chains at specific positions. In contrast with previous research [48], mutations of Ser65 did not affect anion permeation. Presumably, therefore, Ser65 (Ser103) is part of the channel-opening mechanism but not of the permeation pathway. As the permeation pathway accounted for all known functional properties of EAAT/GltPh anion channels during simulations, it is the most likely mechanism of uncoupled chloride conductance.

AB - It has come to the attention of the authors that a citation for Figure 4 was omitted from the caption. The caption should read: Figure 4. Predicted anion permeation pathway. A GltPh monomer viewed from the trimerization interface. The residues R276 and M395 responsible for the anion selectivity are indicated. The orange circles represent 'snapshots' of the path of a chloride ion through the channel between the two domains. Part of the scaffold domain has been removed for clarity. Figure adapted from [49]. Additionally, some references were incorrectly cited in the second paragraph of the section 'Uncoupled Chloride Conductance'. The paragraph should read: Initially, chloride permeation was proposed to occur along TM2 [47]. The Ser to Val mutation on TM2 (residue 65 in GltPh and 103 in EAAT1) strongly affected chloride permeation [8,47]. The GltPh structure in an intermediate OFC suggested that there was an aqueous cavity that might serve as a permeation pathway for anions [14]. Subsequent research has suggested that substrate transport and anion permeation proceed through two mutually exclusive pathways separated by a flexible wall domain and facilitated by the conformational changes [48,49]. The moving flexible wall is composed of several residues in HP1, HP2 hairpins and TM8 (Figure 4), the movement of which dictate the pathway [49]. Arg276 in HP1 and Met395, predicted to line the anion pore [49], were shown to exhibit a significant Cl-selectivity over Na+ in both simulations and experiments: Anion selectivity is impaired by the insertion of negatively charged side chains at specific positions. In contrast with previous research [48], mutations of Ser65 did not affect anion permeation. Presumably, therefore, Ser65 (Ser103) is part of the channel-opening mechanism but not of the permeation pathway. As the permeation pathway accounted for all known functional properties of EAAT/GltPh anion channels during simulations, it is the most likely mechanism of uncoupled chloride conductance.

UR - https://www.scopus.com/pages/publications/85074379654

U2 - 10.1042/BST-2019-0316_COR

DO - 10.1042/BST-2019-0316_COR

M3 - Comment/debate

C2 - 31488571

AN - SCOPUS:85074379654

SN - 0300-5127

VL - 47

SP - 1567

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - 5

ER -