The beta-thymosins are a highly conserved family of small polar peptides known to bind monomeric actin and inhibit its polymerization. The beta-thymosins show a high degree of sequence conservation among all vertebrate classes and they have been also identified in some invertebrate phyla. The most abundant beta-thymosins in mammals are thymosin beta4 (Tbeta4) and thymosin beta10 (Tbeta10), two ubiquitous small (43 amino acids) peptides sharing a high degree of sequence homology. Both beta-thymosins are present in virtually all mammalian tissues and cells studied, showing distinct patterns of expression in several tissues. The beta-thymosins are expressed in the developing and mature nervous system, indicating their participation with other actin-binding peptides in the control of actin polymerization. In the rat cerebellum the temporal and cellular patterns of expression of Tbeta4 and Tbeta10 are different, suggesting that each beta-thymosin could play a specific physiological function during cerebellum development. The possible roles of beta-thymosins in the developing mammalian cerebellum are discussed.