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J Biol Chem, Vol. 275, Issue 18, 13933-13939, May 5, 2000
From the ADAM12 belongs to the transmembrane
metalloprotease ADAM ("a disintegrin and metalloprotease") family.
ADAM12 has been implicated in muscle cell differentiation and fusion,
but its precise function remains unknown. Here, we show that ADAM12 is
dramatically up-regulated in regenerated, newly formed fibers in
vivo. In C2C12 cells, ADAM12 is expressed at low levels in
undifferentiated myoblasts and is transiently up-regulated at the onset
of differentiation when myoblasts fuse into multinucleated myotubes,
whereas other ADAMs, such as ADAMs 9, 10, 15, 17, and 19, are expressed
at all stages of differentiation. Using the yeast two-hybrid screen, we
found that the muscle-specific
Binding of ADAM12, a Marker of Skeletal Muscle Regeneration,
to the Muscle-specific Actin-binding Protein,
-Actinin-2, Is
Required for Myoblast Fusion*
§,¶,
,,
Burnham Institute, La Jolla Cancer Research
Center, La Jolla, California 92037 and the ** Institute of Molecular
Pathology, University of Copenhagen, Frederik V's VEJ 11, 2100 Copenhagen, Denmark
-actinin-2 strongly binds to the
cytoplasmic tail of ADAM12. In vitro binding assays with
GST fusion proteins confirmed the specific interaction. The major
binding site for -actinin-2 was mapped to a short sequence in the
membrane-proximal region of ADAM12 cytoplasmic tail; a second binding
site was identified in the membrane-distal region.
Co-immunoprecipitation experiments confirm the in vivo
association of ADAM12 cytoplasmic domain with -actinin-2.
Overexpression of the entire cytosolic ADAM12 tail acted in a dominant
negative fashion by inhibiting fusion of C2C12 cells, whereas
expression of a cytosolic ADAM12 lacking the major -actinin-2
binding site had no effect on cell fusion. Our results suggest that
interaction of ADAM12 with -actinin-2 is important for ADAM12 function.
*
This work was supported by grants from the National
Institutes of Health and Muscular Dystrophy Association (to E. E.) and by the Danish Medical Research Council (to U. M. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: BioInvent Therapeutic AB, Sölvegatan
41, 223 70 Lund, Sweden.
To whom correspondence should be addressed: Burnham Institute,
La Jolla Cancer Research Center, 10901 N. Torrey Pines Road, La Jolla,
CA 92037. Tel.: 858-646-3100; Fax: 858-646-3199; E-mail: eengvall@burnham.org.
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