Centrins are subfamily within the superfamily of Ca²⁺-modulated proteins that play a fundamental role in centrosome duplication and contraction of centrin-based fiber system. We were mainly devoted to researching the fiber-contraction function of centrin. The recent progress made in the assemble multimers or even in the filamentous network from the recombinant protein produced in Escherichia coli provide a new understanding of the mechanism of the interaction and the force between the proteins. In this paper, we reviewed the reported results including ours, and found that the widely used term “polymerization” is not a proper characterization of the interaction process from the thermal effect, the reversible characteristic, and especially the interaction nature of centrin self-assembly. Compared with the well-accepted polymerizing protein, actin, we conclude that the self-assembly of centrin should be Ca²⁺ modulated transient protein aggregation.