Anti-CCDC89 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

CCDC89 also known as coiled-coil domain containing 89 is a protein with a molecular mass of approximately 33 kDa. It is expressed in various tissues including heart kidney and liver. The protein structure features distinctive coiled-coil domains enabling it to perform mechanical roles in cellular environments. These domains typically facilitate protein-protein interactions important for the wide range of cellular activities that CCDC89 might be involved in.

Biological function summary

CCDC89 participates in processes that influence cell structure and function. It does not act in isolation; instead it associates with other proteins to form complexes that regulate these cellular processes. Scientific evidence suggests its role in cytoskeletal organization making it an important player in maintaining cellular integrity and function. The protein's interaction with other cytoskeletal components underlines its influence in the biological processes occurring within the cell.

Pathways

CCDC89 is integrated into the cytoskeletal signaling pathway powering coordinated cellular dynamics. It interacts closely with proteins such as tubulin which is central to microtubule formation and actin which is essential for the formation of various filament structures. By participating in these pathways CCDC89 contributes to the regulation of the cytoskeleton impacting cellular functions like division movement and shape maintenance.

Associated diseases and disorders

Disruptions involving CCDC89 have been linked to cardiac hypertrophy and polycystic kidney disease. Research indicates that alterations in CCDC89 expression or function can lead to imbalances in cytoskeletal dynamics resulting in pathological states. In cardiac hypertrophy abnormal signaling can occur alongside proteins like titin contributing to maladaptive heart muscle growth. Similarly in polycystic kidney disease its interactions with polycystin proteins might influence abnormal cell proliferation that characterizes this disorder.