Abstract
Gap junction channels are intercellular channels that mediate the gated transfer of molecules between adjacent cells. To identify the domain determining channel conductance, the .rst transmembrane segment (M1) was reciprocally exchanged between Cx46 and Cx32E143. The resulting chimeras exhibited conductances similar to that of the respective M1 donor. Furthermore, a chimera with the carboxy-terminal half of M1 in Cx46 replaced by that of Cx32 exhibited a conductance similar to that of Cx32E143, whereas the chimera with only the amino-terminal half of M1 replaced retained the unitary conductance of wild-type Cx46. Extending the M1 domain swapping to other connexins by replacing the carboxy-terminal half of M1 in Cx46 with that of Cx37 yielded a chimera channel with increased unitary conductance close to that of Cx37. Furthermore, a point mutant of Cx46, with leucine substituted by glycine in position 35, displayed a conductance much larger than that of the wild type. Thus, the M1 segment, especially the second half, contains important determinants of conductance of the connexin channel.
| Original language | English |
|---|---|
| Pages (from-to) | 140-150 |
| Number of pages | 11 |
| Journal | Biophysical Journal |
| Volume | 90 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 2006 |
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ASJC Scopus subject areas
- Biophysics
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Conductance of connexin hemichannels segregates with the first transmembrane segment. / Hu, Xinge; Ma, Meiyun; Dahl, Gerhard.
In: Biophysical Journal, Vol. 90, No. 1, 01.01.2006, p. 140-150.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Conductance of connexin hemichannels segregates with the first transmembrane segment
AU - Hu, Xinge
AU - Ma, Meiyun
AU - Dahl, Gerhard
PY - 2006/1/1
Y1 - 2006/1/1
N2 - Gap junction channels are intercellular channels that mediate the gated transfer of molecules between adjacent cells. To identify the domain determining channel conductance, the .rst transmembrane segment (M1) was reciprocally exchanged between Cx46 and Cx32E143. The resulting chimeras exhibited conductances similar to that of the respective M1 donor. Furthermore, a chimera with the carboxy-terminal half of M1 in Cx46 replaced by that of Cx32 exhibited a conductance similar to that of Cx32E143, whereas the chimera with only the amino-terminal half of M1 replaced retained the unitary conductance of wild-type Cx46. Extending the M1 domain swapping to other connexins by replacing the carboxy-terminal half of M1 in Cx46 with that of Cx37 yielded a chimera channel with increased unitary conductance close to that of Cx37. Furthermore, a point mutant of Cx46, with leucine substituted by glycine in position 35, displayed a conductance much larger than that of the wild type. Thus, the M1 segment, especially the second half, contains important determinants of conductance of the connexin channel.
AB - Gap junction channels are intercellular channels that mediate the gated transfer of molecules between adjacent cells. To identify the domain determining channel conductance, the .rst transmembrane segment (M1) was reciprocally exchanged between Cx46 and Cx32E143. The resulting chimeras exhibited conductances similar to that of the respective M1 donor. Furthermore, a chimera with the carboxy-terminal half of M1 in Cx46 replaced by that of Cx32 exhibited a conductance similar to that of Cx32E143, whereas the chimera with only the amino-terminal half of M1 replaced retained the unitary conductance of wild-type Cx46. Extending the M1 domain swapping to other connexins by replacing the carboxy-terminal half of M1 in Cx46 with that of Cx37 yielded a chimera channel with increased unitary conductance close to that of Cx37. Furthermore, a point mutant of Cx46, with leucine substituted by glycine in position 35, displayed a conductance much larger than that of the wild type. Thus, the M1 segment, especially the second half, contains important determinants of conductance of the connexin channel.
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U2 - 10.1529/biophysj.105.066373
DO - 10.1529/biophysj.105.066373
M3 - Article
C2 - 16214855
AN - SCOPUS:33646137561
VL - 90
SP - 140
EP - 150
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 1
ER -