cdc-48.2 Antibody

CDC-48.2 is an ATP-dependent chaperone that utilizes the energy derived from ATP hydrolysis to generate mechanical force. This force is used for various cellular processes, including unfolding substrate proteins, disassembling protein complexes, and disaggregating protein aggregates. Notably, CDC-48.2 can also prevent aggregation of unfolded proteins in an ATP-independent manner. It targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. This function is crucial for the cytoplasmic elimination of misfolded proteins exported from the endoplasmic reticulum (ER). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER. In conjunction with UDF-2 and CHN-1, CDC-48.2 regulates myosin assembly in body wall muscles by targeting the myosin chaperone UNC-45 for proteasomal degradation. During oocyte meiosis, CDC-48.2, along with CDC-48.1, plays a critical role in chromosome condensation at the diakinesis phase of prophase I and the progression of metaphase I. During the first embryonic cell division, CDC-48.2 regulates DNA replication, ensuring proper chromosome segregation, decondensation, and nuclear envelope re-assembly. In S phase, CDC-48.2, in association with UFD-1, NPL-4.1/NPL-4.2, and UBXN-3, promotes the degradation of DNA licensing factor CDT-1 after the initiation of DNA replication. This process leads to the disassembly of the DNA replication CMG helicase complex by facilitating the dissociation of several of its components from chromatin, including CDC-45 and SLD-5. Furthermore, CDC-48.2 regulates UBXN-3 nuclear localization during S phase. During the first embryonic cell divisions, in collaboration with CDC-48.1, CDC-48.2 regulates the re-assembly of the nuclear envelope after mitosis. This process is likely achieved by inactivating the kinase AIR-2, a component of the chromosomal passenger complex (CPC).