| ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:18854144, PubMed:18782221, PubMed:22768338). Can also prevent aggregation of unfolded proteins also in an ATP- independent manner (PubMed:18782221). Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains (PubMed:19545544). Involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). In association with helicase him-6 and GTPase crp-1, regulates the unfolded protein response (UPR) following ER stress, probably independently of the ERAD pathway (PubMed:18458060). Together with udf-2 and chn-1, regulates myosin assembly in body wall muscles by targeting myosin chaperone unc- 45 for proteasomal degradation (PubMed:17369820). Together with the ufd-1-npl-4 complex, controls the switch from spermatogenesis to oogenesis by regulating E3 ligase cul-2 complex-mediated tra-1 proteasomal degradation (PubMed:19773360). During oocyte meiosis and together with cdc-48.2, required for chromosome condensation at the diakinesis phase in prophase I and for progression of metaphase I (PubMed:17512499). During the first embryonic cell division, regulates DNA replication and thus chromosome segregation and decondensation, and nuclear envelope re-assembly (PubMed:18097415, PubMed:18854144, PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). In S phase and in association with ufd-1, npl-4.1 and/or npl-4.2 and ubxn- 3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:21981920, PubMed:26842564, PubMed:28368371). Regulates ubxn-3 nuclear localization during S phase (PubMed:26842564). During the first embryonic cell divisions and together with cdc-48.2, regulates the re- assembly of the nuclear envelope after mitosis possibly by inactivating kinase air-2, a component of the chromosomal passenger complex (CPC) (PubMed:18097415). However, in another study, cdc-48.1 does not appear to be implicated in the regulation of air-2 (PubMed:18854144). {Experimental EvidencePubMed:16647269, Experimental EvidencePubMed:17369820, Experimental EvidencePubMed:17512499, Experimental EvidencePubMed:17825049, Experimental EvidencePubMed:18097415, Experimental EvidencePubMed:18458060, Experimental EvidencePubMed:18728180, Experimental EvidencePubMed:18782221, Experimental EvidencePubMed:18854144, Experimental EvidencePubMed:19545544, Experimental EvidencePubMed:19773360, Experimental EvidencePubMed:21317884, Experimental EvidencePubMed:21981920, Experimental EvidencePubMed:22768338, Experimental EvidencePubMed:25652260, Experimental EvidencePubMed:26842564, Experimental EvidencePubMed:28368371}. |
National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory