Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions. 2011

Karen I Brackley, and Julie Grantham
Department of Cell and Molecular Biology, Göteborgs Universitet, Medicinaregatan 9C, Gothenburg, Sweden.

CCT is a member of the chaperonin family of molecular chaperones and consists of eight distinct subunit species which occupy fixed positions within the chaperonin rings. The activity of CCT is closely linked to the integrity of the cytoskeleton as newly synthesized actin and tubulin monomers are dependent upon CCT to reach their native conformations. Furthermore, an additional role for CCT involving interactions with assembling/assembled microfilaments and microtubules is emerging. CCT is also known to interact with other proteins, only some of which will be genuine folding substrates. Here, we identify the actin filament remodeling protein gelsolin as a CCT-binding partner, and although it does not behave as a classical folding substrate, gelsolin binds to CCT with a degree of specificity. In cultured cells, the levels of CCT monomers affect levels of gelsolin, suggesting an additional link between CCT and the actin cytoskeleton that is mediated via the actin filament severing and capping protein gelsolin.

UI MeSH Term Description Entries
D008841 Actin Cytoskeleton Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments. Actin Filaments,Microfilaments,Actin Microfilaments,Actin Cytoskeletons,Actin Filament,Actin Microfilament,Cytoskeleton, Actin,Cytoskeletons, Actin,Filament, Actin,Filaments, Actin,Microfilament,Microfilament, Actin,Microfilaments, Actin
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017434 Protein Structure, Tertiary The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D017510 Protein Folding Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D056404 Chaperonin Containing TCP-1 A group II chaperonin found in eukaryotic CYTOSOL. It is comprised of eight subunits with each subunit encoded by a separate gene. This chaperonin is named after one of its subunits which is a T-COMPLEX REGION-encoded polypeptide. CCT delta Subunit,Chaperonin CCT,Chaperonin CCT, alpha Subunit,Chaperonin CCT, beta Subunit,Chaperonin CCT, delta Subunit,Chaperonin CCT, epsilon Subunit,Chaperonin CCT, eta Subunit,Chaperonin CCT, gamma Subunit,Chaperonin CCT, theta Subunit,Chaperonin CCT, zeta1 Subunit,Chaperonin CCT, zeta2 Subunit,Chaperonin Containing TCP1, Subunit 1,Chaperonin Containing TCP1, Subunit 2,Chaperonin Containing TCP1, Subunit 3,Chaperonin Containing TCP1, Subunit 4,Chaperonin Containing TCP1, Subunit 5,Chaperonin Containing TCP1, Subunit 6A,Chaperonin Containing TCP1, Subunit 6B,Chaperonin Containing TCP1, Subunit 7,Chaperonin Containing TCP1, Subunit 8,Chaperonin Containing t-Complex Polypeptide,Chaperonin-Containing T-Complex Polypeptide 1,Cytosolic Chaperonin,Cytosolic Molecular Chaperone CCT,Testis Complex Polypeptide 1,t-Complex Polypeptide 1,t-Complex Protein 1,Chaperonin Containing T Complex Polypeptide 1,Chaperonin Containing TCP 1,Chaperonin Containing t Complex Polypeptide,Chaperonin, Cytosolic,t Complex Polypeptide 1,t Complex Protein 1
D018260 Gelsolin A 90-kDa protein produced by macrophages that severs ACTIN filaments and forms a cap on the newly exposed filament end. Gelsolin is activated by CALCIUM ions and participates in the assembly and disassembly of actin, thereby increasing the motility of some CELLS. Gelsolin Protein,Serum Actin Inhibitory Protein
D034741 RNA, Small Interfering Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions. RNA, Scan,Repeat-Associated siRNA,Scan RNA,Small Scan RNA,Trans-Acting siRNA,siRNA,siRNA, Repeat-Associated,siRNA, Trans-Acting,Short Hairpin RNA,Short Interfering RNA,Small Hairpin RNA,Small Interfering RNA,scnRNA,shRNA,tasiRNA,Hairpin RNA, Short,Hairpin RNA, Small,Interfering RNA, Short,Interfering RNA, Small,RNA, Short Hairpin,RNA, Short Interfering,RNA, Small Hairpin,RNA, Small Scan,Repeat Associated siRNA,Scan RNA, Small,Trans Acting siRNA,siRNA, Repeat Associated,siRNA, Trans Acting
D041702 BALB 3T3 Cells Cell lines developed from disaggregated BALB/c mouse embryos. They are extremely sensitive to CONTACT INHIBITION, and highly susceptible to transformation by SV40 VIRUS and murine sarcoma virus (SARCOMA VIRUSES, MURINE). 3T3 Cells, BALB,BALB 3T3 clone A31,BALB-3T3 Cells,BALB-c 3T3 Cells,3T3 Cell, BALB,3T3 Cell, BALB-c,3T3 Cells, BALB-c,BALB 3T3 Cell,BALB c 3T3 Cells,BALB-3T3 Cell,BALB-c 3T3 Cell,Cell, BALB 3T3,Cell, BALB-3T3,Cell, BALB-c 3T3,Cells, BALB 3T3,Cells, BALB-3T3,Cells, BALB-c 3T3

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