A new job for ancient extracellular matrix proteins: Hemicentins stabilize cleavage furrows

Commun Integr Biol. 2011 Jul;4(4):433-5. doi: 10.4161/cib.4.4.15324. Epub 2011 Jul 1.


Interactions between extracellular matrix (ECM) proteins and transmembrane receptors mediate changes in cell shape during cell migration, adhesion, differentiation and polarization. Cytokinesis is the final step in cell division as cells employ a contractile ring composed of actin and myosin to partition one cell into two. During the partition process, an invagination in nascent membrane forms a new extracellular space called the cleavage furrow. Despite the dramatic changes in cell shape during cytokinesis, existing models include no role for the ECM. In a recent paper, we show that hemicentins assemble in the cleavage furrow of C. elegans germ cells and mouse embryo blastomeres. Hemicentin depletion results in membrane destabilization, cleavage furrow retraction and cytokinesis failure. The data suggest that hemicentins and other ECM proteins stabilize the cleavage furrow during cytokinesis of multiple cell types.

Keywords: Caenorhabditis elegans; cleavage furrow; cytokinesis; extracellular matrix; hemicentin; mouse embryo.