Myristoylated alanine-rich kinase C substrate (MARCKS), an actin-binding protein, is involved in several signal transduction pathways. It is susceptible to be phosphorylated by protein kinases as protein kinase C and some proline-directed kinases. These phosphorylations differently modulate its functions. We previously showed that a phosphorylation at its Ser25 (S25p-MARCKS) in chickens is a signature of this ubiquitous protein in neuron differentiation. To gain insight into the possible involvement of MARCKS in late retinal histogenesis, we compared the developmental expression patterns of the total protein and its S25p variants. Here we show that the most outstanding modifications occur at the outer retina, where S25p disappears at the end of embryonic development and where MARCKS is missing in adults. These results suggest diverse functional specializations in the different retinal layers.