It is 30 years since Ebashi and colleagues showed that Ca2+ ions direc
tly affect regulation of the myosin-actin interaction in muscle throug
h the action of tropomyosin and troponin on muscle thin filaments. It
is more than 20 years since the idea was put forward that tropomyosin
mig ht act, at least in part, by changing its position on actin, thus
uncovering or modifying the myosin binding site on actin when troponin
molecules take up Ca2+. Since that time, a great deal of evidence for
and against this steric blocking mechanism has been published: a stru
cture for actin filaments at close to atomic resolution has been propo
sed, and the whole regulation story has become both more complicated a
nd more subtle. Here we review structural and biochemical aspects of r
egulation in vertebrate skeletal muscle. We show that some basic ideas
of the steric blocking mechanism remain valid. We also show that addi
tional factors, such as troponin movements and structural changes with
in the actin monomers themselves, may be crucial, A number of the resu
lting regulation scenarios need to be distinguished.-Squire, J. M., Mo
rris, E. P. A new look at thin filament regulation in vertebrate skele
tal muscle.