dynein light chain (DLC)-like domain found in cytoplasmic dynein light chain 1 (DYNLL1), axonemal dynein light chain 4 (DNAL4), tegumental-allergen-like proteins (TALs) and similar proteins
The family includes cytoplasmic dynein light chain 1 (DYNLL1), DYNLL2, axonemal dynein light chain 4 (DNAL4), and tegumental-allergen-like proteins (TALs). DYNLL1, also called protein inhibitor of neuronal nitric oxide synthase (PIN), or 8 kDa dynein light chain (DLC8), or dynein light chain LC8-type 1 (DLC1), is one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. It acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. It may play a role in changing or maintaining the spatial distribution of cytoskeletal structures. DYNLL2, also called cytoplasmic dynein light chain 2, or 8 kDa dynein light chain b (DLC8b), or dynein light chain LC8-type 2 (DLC2), is one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. DNAL4 is a force generating protein of respiratory cilia. It produces force towards the minus ends of microtubules. TALs, also called tegument antigens, are characterized by two N-terminal EF-hand motifs and a C-terminal region resembling a dynein light chain (DLC)-like domain. They were mainly found in parasitic platyhelminth species. TALs are strongly associated with the tegument, a syncytial structure that forms the outer layer of the organism. They may be involved in the transport of vesicles within the tegumental cytoplasm, probably within dynein motor complexes.
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