Analogous standard motifs in myelin basic protein and in MARCKS

Myelin basic protein (MBP) and myristoylated alanine-rich C-kinase substrat e (MARCKS) are similar in terms of having extended conformations regulated by their environment (i.e., solubilised or lipid-associated), N-terminal mo difications, a dual nature of interactions with lipids, binding to actin an d Ca2+-calmodulin, and being substrates for different kinds of protein kina ses. The further sequence similarities of segments of MBP with lipid effect or regions of MARCKS, and numerous reports in the literature, support the t hesis that some developmental isoform of MBP functions in signal transducti on.