Although deletion of one of the alpha-tubulin genes, tubB, was possible, this strain was subsequently unable to reproduce sexually; this defect was partially overcome via overexpression of tubA. These results demonstrate nicely overlapping but also distinct functions of certain tubulin isoforms; however, this picture becomes further complicated by the fact that a number of different posttranslational MT modifications exist. Already in 1975, Arce et al. reported the posttranslational incorporation of L-tyrosine into alpha-tubulin, indicating the presence of tyrosinated and detyrosinated MT forms. alphatubulin generally ends with the tripeptide EEY, and the tyrosine residue is cyclically removed by carboxypeptidase, then re-added to the chain by tubulin-tyrosine ligase. Other possible modifications include acetylation, polyglutamylation, polyglycylation or phosphorylation. In general, little is known about either modifying enzymes or the biological functions of these modifications, although the suppression of tubulin tyrosine ligase and subsequent accumulation of detyrosinated tubulin favors tumor growth in animal models and human cancers. In neurons it was demonstrated that polarized trafficking of kinesin-1-driven vesicle movement is regulated through the balance between tyrosinated and detyrosinated MTs. Since somatodendrites contain tyrosinated alpha-tubulin and the axon contains detyrosinated alpha-tubulin, inhibited binding of kinesin1 to tyrosinated MTs restricted the transport function to the axons. In this case, the b5-L8 region in the motor domain was responsible for MT discrimination. In contrast, we show that in A. nidulans the 86 amino acid long region in the tail of kinesin-3 UncA was involved in the recognition process of modified, possibly detyrosinated MTs. Interestingly, UncA cargoes appear to be un-involved in MT recognition, since deletion of the PH domain did not alter its specificity. In comparison, there is evidence that mammalian kinesin-1 cargo proteins may be involved in specificity determination in neuronal cells. Unfortunately, no structural data are available yet for the tail of a kinesin-3 motor protein, because only the motor domain and its binding to MTs has been analyzed. In comparison to our data, it was shown in mice that kinesin-3 uses polyglutamylation as a neural molecular traffic sign, although the structural mechanism of the kinesin remained enigmatic. The picture becomes increasingly complex when considering the recent observation that the modification type may switch from detyrosination to acetylation upon polarization of epithelial cells. It will be the challenge for future Alisol-B studies to unravel the exact mechanism of motor proteins for MT discrimination between different MTs, and determine how posttranslational modifications contribute to navigational cues for different motor proteins. The novel denomination for RCAN genes and proteins has recently been Licochalcone-C approved by the HUGO Gene Nomenclature Committee, and due to the large number of human RCAN mRNA isoforms, a specific nomenclature was proposed: RCAN1, RCAN2 or RCAN3 – followed by the hitherto identified exon numbers. In particular, calcineurin activation causes nuclear factor of activated T-cells transcription factors translocation to the nucleus, where, in cooperation with other transcription factors, they induce genes expression. A calcineurin inhibitor RCAN motif has been demonstrated to bind calcineurin, whose signalling plays a role in many physiological and pathological processe.