We analyzed the structure of cytoplasmic bridges called ring canals in
Drosophila egg chambers. Two mutations, hu-li tai shao (hts) and kelc
h, disrupt normal ring canal development. We raised antibodies against
the carboxy-terminal tail of hts and found that they recognize a prot
ein that localizes specifically to ring canals very early in ring cana
l assembly. Accumulation of filamentous actin on ring canals coincides
with the appearance of the hts protein. kelch, which is localized to
the ring canals hours after hts and actin, is necessary for maintainin
g a highly ordered ring canal rim since kelch mutant egg chambers have
ring canals that are obstructed by disordered actin and hts. Anti-pho
sphotyrosine antibodies immunostain ring canals beginning early in the
germarium before hts and actin and throughout egg chamber development
. The use of antibody reagents to analyze the structure of wild-type a
nd mutant ring canals has shown that ring canal development is a dynam
ic process of cytoskeletal protein assembly, possibly regulated by tyr
osine phosphorylation of some ring canal components.