Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.6.1.3 (
ATPase
)
65,361
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Fesselin is an actin binding protein that bundles actin filaments and accelerates nucleation of actin polymerization. The effect of
fesselin
on actin polymerization is regulated by Ca(++)-calmodulin. Because actin filaments serve both structural and contractile functions we also examined the effect of
fesselin
on activation of myosin S1
ATPase
activity. Fesselin inhibited the activation of S1-catalyzed ATP hydrolysis in a similar manner in both the presence and absence of tropomyosin. This inhibition was unaffected by Ca(++)-calmodulin. Fesselin inhibited the binding of myosin-S1 to actin during steady-state ATP hydrolysis. Fesselin also displaced caldesmon from actin. S1 displaced
fesselin
from actin in the absence of nucleotide when the affinity of S1 for actin was much greater than the affinity of
fesselin
for actin. It is likely that
fesselin
and S1 share common binding sites on F-actin. We also observed that
fesselin
could bind to smooth muscle myosin with muM affinity. Fesselin shares some similarities to caldesmon in binding to several other proteins and having multiple potential functions.
...
PMID:Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity. 1617 73
Fesselin is an actin binding protein from smooth muscle that nucleates actin polymerization in a Ca(++)-calmodulin dependent manner, bundles actin and inhibits the actin-activated
ATPase
activity of myosin S1. We now report that
fesselin
binds to smooth muscle alpha-actinin. Binding was measured by blot overlay, affinity chromatography and sedimentation methods. Binding was moderate with an association constant of 1-4 x 10(7) M(-1) assuming a 1:1 association of
fesselin
with alpha-actinin. Fesselin binds to the central spectrin domain repeat region of alpha-actinin but not to the CH1-CH2 domain. Fesselin accelerates the polymerization of actin. This activity of
fesselin
was attenuated by alpha-actinin. These observations support the role of
fesselin
in organizing the cytoskeleton.
...
PMID:Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization. 1645 54
