In this review, we describe which actin amino acid residues can be selectively oxidized and reduced in many different ways ( e.g. While actin oxidation by reactive oxygen species (ROS) at non-physiological levels are known for long to impact on actin polymerization and on the cellular actin cytoskeleton, growing evidence shows that direct and reversible oxidation/reduction of specific actin amino acids plays an important and physiological role in regulating the actin cytoskeleton. The actin cytoskeleton must be finely tuned, both in space and time, to fulfill key cellular functions such as cell division, cell shape changes, phagocytosis and cell migration. This work was supported by the DFG, an FCI grant, and a scholarship ofĪctin is among the most abundant proteins in eukaryotic cells and assembles into dynamic filamentous networks regulated by many actin binding proteins. Bohn for the vimentin cDNA, and the Kazusa DNA Research Institute, Japan, for providing the human KIAA0819, 0903, and 1668 cDNAs. Bogdan for anti-tubulin and anti-mouse Alexa-568 antibodies, Dr. Ossendorf for critically reading the manuscript. Kremerskothen for help with immunofluorescence analysis and rat tissue extracts, M. The sequences have not been previously published completely however, Terman et al. The high homology between MICAL-1, -2, and -3 is restricted to this region the remaining sequences differ from each other. The previously uncharacterized MICAL-2 and MICAL-3 were discovered by sequence analysis in a BLAST search using the carboxyterminal region, which includes the rab1 binding domain. In this study, we were able to identify further members of the MICAL family as rab1 interaction partners. We cloned the regions corresponding to the rab1 Discussion In order to identify other putative rab1 interacting proteins, we performed a BLAST search with this rab1-binding domain and identified four clones that share a carboxyterminal sequence homology of about 50%: FLJ14966, KIAA0819, KIAA0903, and KIAA1668. The domain essential for the binding was mapped to the carboxyterminal region of MICAL-1. AB051455), Interaction of proteins of the MICAL gene family with rab1Īs we previously reported, MICAL-1 is a specific interaction partner of the small GTPase rab1. These cDNA sequences encode the carboxyterminal domains of the following human proteins: 167aa of MICAL-2 (FLJ14966, Accession No. Constructs were cloned into pGADT7 and pGEX for the yeast two-hybrid and in vitro binding experiments. Corresponding mutants of rab1a, ypt1, and rab6 were used in this study. The rab1b mutants used have been described previously.

Mical biochemical