ABCC7 p.Pro99Cys
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 21594800
[PubMed]
Cai Z et al: "Application of high-resolution single-channel recording to functional studies of cystic fibrosis mutants."
No.
Sentence
Comment
298
However, Akabas et al. (63) concluded that P99 does not line the CFTR pore because the site-directed mutant P99C did not react with methanethiosulfonate reagents.
X
ABCC7 p.Pro99Cys 21594800:298:108
status: NEW
PMID: 21796338
[PubMed]
Qian F et al: "Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant."
No.
Sentence
Comment
140
In this respect, the slow rate of modification observed in N1138C (Fig. 3b) is similar to that we reported for P99C and L102C in TM1 [41] and T338C and S341C in TM6 [9], and the much higher modification rate constant for T1142C, S1141C, and (to a lesser extent) M1140C is closer to that reported for K95C in TM1 [41] and I344C, V345C, and M348C in TM6 [9].
X
ABCC7 p.Pro99Cys 21796338:140:111
status: NEW
No.
Sentence
Comment
128
However, because P99C did(128) could control the pore properties of the CF-associated mutant R347H simply by manipulating pH.
X
ABCC7 p.Pro99Cys 9922375:128:17
status: NEW
PMID: 21746847
[PubMed]
Wang W et al: "Alignment of transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore."
No.
Sentence
Comment
71
In contrast, macroscopic currents carried by four mutants, K95C, Q98C, P99C, and L102C, were found to be significantly and rapidly sensitive to the application of both MTSES and MTSET (Figs. 1-3).
X
ABCC7 p.Pro99Cys 21746847:71:71
status: NEW105 (B) Example leak-subtracted I-V relationships for cys-less CFTR, K95C, Q98C, P99C, L102C, and R104C, recorded from inside-out membrane patches after maximal channel activation with 20 nM PKA, 1 mM ATP, and 2 mM PPi.
X
ABCC7 p.Pro99Cys 21746847:105:77
status: NEW112 As shown in Fig. 4 A, patches excised from MTSET-pretreated cells expressing K95C, Q98C, P99C, or L102C all gave macroscopic currents that were increased in amplitude after the addition of 2 mM constants was that modification was faster for cysteines introduced closer to the intracellular end of TM1, and slower for cysteines located more deeply along the axis of TM1 (Fig. 3 B).
X
ABCC7 p.Pro99Cys 21746847:112:89
status: NEW136 Whereas K95C channels were again rendered insensitive to a test exposure to MTSES, again consistent with them having been covalently modified during pretreatment, currents carried by Q98C, P99C, MTSET to the intracellular solution.
X
ABCC7 p.Pro99Cys 21746847:136:189
status: NEW138 These results suggest that none of K95C, Q98C, P99C, or L102C can be modified covalently by extracellular MTSET.
X
ABCC7 p.Pro99Cys 21746847:138:47
status: NEW141 We used a similar approach to determine if K95C, Q98C, P99C, and L102C could be modified by MTSES pretreatment.
X
ABCC7 p.Pro99Cys 21746847:141:55
status: NEW150 These results, which are summarized quantitatively in Fig. 5 C, suggest that although K95C can be modified by MTSES before channel activation, Q98C, P99C, and L102C are modified by MTSES only very slowly, if at all, in channels that have not been activated by PKA and ATP.
X
ABCC7 p.Pro99Cys 21746847:150:149
status: NEW228 Thus, the side chains of TM1 mutants K95C, Q98C, P99C, and L102C that we identified as accessible to MTS reagents applied from the inside (Fig. 2) were not accessible to MTSET applied to the outside (Fig. 4), whereas R104C, previously shown to be modified by external MTS reagents (Zhou et al., 2008), was not modified by internal MTSES or MTSET (Fig. 2).
X
ABCC7 p.Pro99Cys 21746847:228:49
status: NEW238 Although we have not investigated the state dependence of MTSES modification in TM1 in such great detail, our present results suggest a similar arrangement in which K95C can readily be modified before channel activation (Fig. 5), whereas Q98C, P99C, and L102C are modified rapidly after channel activation (Fig. 3) but very slowly if at all before activation (Fig. 5).
X
ABCC7 p.Pro99Cys 21746847:238:244
status: NEW256 For comparison, the MTSES modification rate constant for P99C and L102C (Fig. 3) was similar to that of T338C and S341C in TM6 (El Hiani and Linsdell, 2010) (all between 100 and 150 M1 s1 ), and the modification rate constant for K95C was comparable to, or slightly greater than, that of I344C, V345C, and M348C (El Hiani and Linsdell, 2010) (all between 2,000 and 4,000 M1 s1 ).
X
ABCC7 p.Pro99Cys 21746847:256:57
status: NEW
PMID: 8663008
[PubMed]
Sheppard DN et al: "Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function."
No.
Sentence
Comment
204
Because P99C did not react with sulfhydryl-specific reagents, Akabas and collaborators concluded that Pro99 does not line the channel pore (7).
X
ABCC7 p.Pro99Cys 8663008:204:8
status: NEW212 This suggests that the defective processing of the P205S mutant observed in HeLa cells likely accounts for the loss of Cl- channel function in patients bearing this mutation.
X
ABCC7 p.Pro99Cys 8663008:212:8
status: NEW
PMID: 23442957
[PubMed]
Gao X et al: "Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeation."
No.
Sentence
Comment
196
Third, in the report by Wang et al. (35), K95C, but not Q98C, P99C, or L102C, can react with internal MTSES even before the channel is activated by PKA and ATP, implying a regulated barrier between positions 95 and 98.
X
ABCC7 p.Pro99Cys 23442957:196:62
status: NEW263 (A) Representative single-channel traces for WT/Cysless, A96C/ Cysless, I106C/Cysless, and P99C mutant channels.
X
ABCC7 p.Pro99Cys 23442957:263:91
status: NEW