KChannelDB: Extraction of mutation data from the literature

2005, KChannelDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation C185A was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation C185A in IRK5_RAT

Point mutation:	C185A
Cited point mutation:	Cys185Ala,Cys-185
Domain:	TRANSMEM II
General numbering (KChannelDB):	264
Protein:	IRK5_RAT (Kcnj5,Girk)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in IRK5_RAT
Family alignments	Inward rectifiers (Kir) Potassium channels 2 TMs
Other point mutations / same position	Position 160 in Inward rectifiers (Kir) family Position 160 in Potassium channels 2 TMs family
Reference:	Inhibition of G-protein-coupled inward rectifying K+ channels by intracellular acidosis. Mao J, Wu J, Chen F, Wang X, Jiang C J Biol Chem 2003 Feb 28;278(9):7091-8.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

C185A

To address this possibility , we took advantage of two mutants that are defective in G-protein-dependent channel gating (i.e. GIRK1 / GIRK4C216T , GIRK1C179A / GIRK4C185A) (41 , 42 )
Currents were recorded from oocytes expressing the G beta gamma coupling-defective mutant GIRK1 / GIRK4C216T (A) or the G-protein-independent mutant GIRK1C179A / GIRK4C185A (B) in the same condition as in Fig. 1
Since mutations of cysteine 185 in GIRK4 and cysteine 179 in GIRK1 enable expression of constitutively active heteromeric GIRK1C179A / GIRK4C185A channels (42 ) , it is possible that these cysteine mutations also allow homomeric expressions
When the homomeric GIRK4C185A was studied , the mutant channel was inhibited by intracellular acidification to almost the same degree as the WT channels (34.7 ą 3.6% , n = 5 , Fig. 3 A)
Thereafter , we decided to perform further studies using the homomeric GIRK4C185A channel
Homomeric expression of GIRK4 channels was made by mutating Cys-185 to alanine (GIRK4C185A)
Consistent with their effects on the homomeric GIRK4C185A , mutation of any of the His-64 , His-228 , or His-352 in GIRK4 disrupted the pH i sensitivity of the heteromeric channels
First , both GIRK1 / GIRK4C216T and GIRK1C179A / GIRK4C185A are equally sensitive to pH i as the WT GIRK1 / GIRK4
Mutation of any of them totally abolished or greatly diminished the pH i sensitivity of the homomeric GIRK4C185A and the heteromeric GIRK1 / GIRK4

Cys-185

Homomeric expression of GIRK4 channels was made by mutating Cys-185 to alanine (GIRK4C185A)

F.Horn (kchanneldbcmbi.ru.nl), 17-Aug-2005