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Vol. 10, Issue 10, 3137-3150, October 1999
*Istituto di Biologia Cellulare, Consiglio Nazionale delle
Richerche, 00137 Rome, Italy; and Rho family GTPases have been implicated in the regulation of the
actin cytoskeleton in response to extracellular cues and in the
transduction of signals from the membrane to the nucleus. Their role in
development and cell differentiation, however, is little understood.
Here we show that the transient expression of constitutively active
Rac1 and Cdc42 in unestablished avian myoblasts is sufficient to cause
inhibition of myogenin expression and block of the transition to the
myocyte compartment, whereas activated RhoA affects myogenic
differentiation only marginally. Activation of c-Jun N-terminal kinase
(JNK) appears not to be essential for block of differentiation because,
although Rac1 and Cdc42 GTPases modestly activate JNK in quail
myoblasts, a Rac1 mutant defective for JNK activation can still inhibit
myogenic differentiation. Stable expression of active Rac1, attained by infection with a recombinant retrovirus, is permissive for terminal differentiation, but the resulting myotubes accumulate severely reduced
levels of muscle-specific proteins. This inhibition is the consequence
of posttranscriptional events and suggests the presence of a novel
level of regulation of myogenesis. We also show that myotubes
expressing constitutively active Rac1 fail to assemble ordered
sarcomeres. Conversely, a dominant-negative Rac1 variant accelerates
sarcomere maturation and inhibits v-Src-induced selective disassembly
of I-Z-I complexes. Collectively, our findings provide a role for Rac1
during skeletal muscle differentiation and strongly suggest that Rac1
is required downstream of v-Src in the signaling pathways responsible
for the dismantling of tissue-specific supramolecular structures.
Dipartimento di
Neuroscienze and Istituto Nazionale di Fisica della Materia, sez
B, Università di Tor Vergata, 00133 Rome, Italy
Corresponding author. E-mail address:
alema{at}ibc.rm.cnr.it.
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