IndraLab

Statements

NTS acetylates CALM1. 5 / 5
| 5
sparser
"Thus, the disruption on CaM dynamics and endocytic function observed in naa15∆ cells is specifically due to lack of Nt‐acetylation of Cam1."
35100446
sparser
"Second, Nt-acetylated Cam1."
31566560
sparser
"This indicates that Nt‐acetylation of Cam1 increases the affinity for binding to Myo1 IQ domains, specifically affinity of the second molecule of Cam1."
35100446
sparser
"To explore whether Cam1 Nt‐acetylation affects this interaction, changes in FRET signal of the Myo1 IQ12 ‐FRET protein induced by binding of half saturating concentrations of Cam1 (2.5 µ m of Cam1, 0.80 µ m of ACE Cam1) were observed over a range of pCa conditions."
35100446
sparser
"To confirm whether the differences observed in calmodulin dynamics is specifically due to Nt‐acetylation of Cam1 alone, or a consequence of Nt‐acetylation of other proteins, equivalent comparative analyses were undertaken betweennaa15 + and naa15∆ cells expressing GFP‐Cam1 [ xref ]."
35100446