IndraLab

Statements

KCNH1 binds CALM. 21 / 32
| 12 9
reach
"Mutations at these sites completely abolished CaM binding to hEAG1."
20523736
reach
"This indicates that the C-terminus of hEAG1 only binds CaM in its Ca 2+ -bound state."
20523736
sparser
"Intracellular calcium at nanomolar concentrations inhibits eag1 currents through calmodulin binding to the eag1 C-terminus [46] , the binding is calcium dependent with an apparent K D of 480 nM."
16473665
reach
"The combined four mutations F151S, A152S, F714S, F717S are therefore sufficient to hinder the binding of CaM to hEAG1 (p> 0.05) BD-C1 and other auxiliary sites can still be involved in the binding mechanism in a cooperative manner."
20523736
reach
"We conclude that these two CaM binding sites, the high-affinity 1-8-14 CaM binding domain in the N-terminus and the previously described C-terminal binding domain at AA 707-276, are the major binding sites involved in CaM binding to EAG1."
20523736
reach
"Mutations at these two sites completely abolished CaM binding to hEAG1, indicating that the BD-N and BD-C2 binding domains are required for CaM binding."
28367272
reach
"The recent CaM bound cryo-EM structure model of rat EAG1 channels provided more detailed information [XREF_BIBR]."
28367272
reach
"The further inspection of CaM bound EAG1 structure showed that all three previously identified CaM binding sites are occupied by one CaM and four CaM molecules are bound to the functional tetramer channel."
28367272
sparser
"An important breakthrough provided by the new structures is the demonstration that: (i) the initial hERG N-tail is positioned in close contact with the S4–S5 and the C-linkers (that are directly attached to the carboxy terminus of the S4 and S6 helices, respectively) and with the long S2–S3 linker (a conserved feature of the KCNH channel family) [ xref , xref , xref ] ( xref ), and (ii) although non-domain swapping exists in the VSD region of eag1 and hERG, an extensive domain swapping exists within the cytoplasmic regions, and this is increased in the case of eag1 trough interaction with CaM, which in conjunction with domain swapping between N- and C-termini establishes a bridge, encompassing three subunits ( xref )."
30634573
sparser
"CaM binds Eag1 in the presence of Ca 2+ and inhibits ion conduction ( xref ) ( xref , xref )."
27516594
sparser
"The basis for this effect is observed in the structure of Eag1 bound to CaM as the closed pore is decoupled from the up or depolarized VS ( xref , xref )."
27516594
sparser
"The binding of CaM to hEAG1 is, in contrast to Ca(2+)-activated potassium channels, Ca(2+) dependent, with an apparent K(D) of 480 nM."
10880439
reach
"As depicted in Fig. 13, our protein docking model supports the idea that 14-3-3θ homodimer interacts with Eag1 in a manner analogous to the well-characterized binding of calmodulin to Eag1 [36, 57]."
36717938
sparser
"Mutations at these two sites completely abolished CaM binding to hEAG1, indicating that the BD-N and BD-C2 binding domains are required for CaM binding."
28367272
reach
"The binding of CaM to hEAG1 is, in contrast to Ca (2+)-activated potassium channels, Ca (2+) dependent, with an apparent K (D) of 480 nM."
10880439
reach
"CaM binds Eag1 in the presence of Ca 2+ and inhibits ion conduction (XREF_FIG)."
27516594
sparser
"As depicted in Fig.  xref , our protein docking model supports the idea that 14-3-3θ homodimer interacts with Eag1 in a manner analogous to the well-characterized binding of calmodulin to Eag1 [ xref , xref ]."
36717938
sparser
"Overall, similar to the presence of four calmodulin molecules interacting with an Eag1 tetramer, we propose that four 14-3-3θ homodimers are bound to the Eag1 tetramer (Fig.  xref D)."
36717938
reach
"The basis for this effect is observed in the structure of Eag1 bound to CaM as the closed pore is decoupled from the up or depolarized VS (XREF_FIG, XREF_FIG)."
27516594
sparser
"Indeed, the N- and C-terminal domains of hEag1 interacts with calmodulin (Schönherr et al., xref ; Ziechner et al., xref ; Gonçalves and Stühmer, xref ), cortactin (Herrmann et al., xref ); KCa3.1 channels interact with ERK1/2 (Millership et al., xref ), and HERG1 channels with the adaptor protein 14-3-3 (Kagan et al., xref ), Src tyrosine kinase (Cayabyab and Schlichter, xref ), and the TNF-α receptor (Wang et al., xref )."
23970866
reach
"CaM binds to Eag1 only in the presence of calcium and holds the pore closed even during membrane depolarization."
31490124