Mucinoprotein is a universal constituent of stable intercellular bridges in Drosophila melanogaster germ line and somatic cells.

Intercellular bridges formed by incomplete cytokinesis may be important in a variety of processes, including synchronization of mitotic and meiotic divisions in animal cells. Using specific antibodies against a mucin-type glycoprotein (Kramerov et al. [1996] FEBS Lett. 378:213-218) from Drosophila melanogaster cultured embryonic cells, we showed that this glycoprotein is located in all cytoplasmic bridges found in various germline and somatic tissues. In the ovary, immunostaining of ring canals connecting germ cells can be detected in the very early stages at the germarium region 1 where first gonial divisions take place, and the immunostaining appears to persist through late stages when transport of cytoplasm from nurse cells to a growing oocyte occurs. Each ring canal is made up of an outer and an inner rim. Mucin glycoprotein appears to be one of the first proteins localized to the outer rim, which is a derivative of the arrested cleavage furrow. The known ring canal proteins, phosphotyrosine-containing protein(s), F-actin, hts- and kelch proteins, are localized to the inner rim at a later developmental time. Similarly, mucin glycoprotein is recruited early to ring canals connecting mitotic primary spermatocytes in both larval and adult testes. Mucin glycoprotein was found to be present in intercellular bridges (small ring canals) in somatic cells, including follicular epithelium in ovary and imaginal disc cells. Intercellular bridges were observed for the first time in a subset of cells in the larval brain. Thus, mucin glycoprotein is the only protein hitherto found in all known types of stable intercellular bridges and may be an important constituent of a backbone needed for assembly and preservation of this particular type of cell-cell contact.