Disease relevance of actin-binding

• We show here that multiple copies of the short actin-binding module CLIK(23) from human or Caenorhabditis elegans calponin proteins effectively inhibit cell motility on two dimensional matrices and suppress soft agar colony formation of metastatic melanoma and adenocarcinoma cells of murine and human origin [1].

High impact information on actin-binding

• These results suggest that spe-26 encodes a cytoskeletal protein, perhaps actin binding, which is necessary to segregate the cellular components that form haploid spermatids [2].
• The s1307 mutation in a putative actin-binding helix caused greater activity in actin-depolymerizing and severing [3].
• To help illuminate this role, we used actin filament affinity chromatography to isolate actin binding proteins from large quantities of Caenorhabditis elegans oocytes [4].
• In an attempt to identify unknown actin-binding proteins in cells of Dictyostelium discoideum that may be involved in the control of cell motility and chemotaxis, monoclonal antibodies were raised against proteins that had been enriched on an F-actin affinity matrix [5].
• The roles of actin-binding proteins in development and morphogenesis are not well understood [6].

Biological context of actin-binding

• The novel flightless-I gene brings together two gene families, actin-binding proteins related to gelsolin and leucine-rich-repeat proteins involved in Ras signal transduction [7].

Anatomical context of actin-binding

• During neuronal development, various actin-binding proteins regulate dynamics of actin cytoskeleton in the growth cones of developing axons [8].
• The molecular domain structure of the protein reveals similarity to the C-terminal repeat region of the smooth muscle actin-binding protein calponin [9].
• Microinjection studies showed that a fusion protein containing the N-terminal actin-binding site localised weakly to stress fibres, whereas one containing the C-terminal site initially localised predominantly to focal adhesions [10].
• MSP-300 is the likely Drosophila ortholog of the mammalian Syne-1 and -2 and C. elegans ANC-1 proteins, contained both actin-binding and nuclear envelope localization domains [11].

Associations of actin-binding with chemical compounds

• Profilins are actin binding proteins, which also interact with polyphosphoinositides and proline-rich ligands [12].

Physical interactions of actin-binding

• The results indicate that C. elegans actin shares common biochemical properties with rabbit muscle actin, while actin-binding proteins can interact with C. elegans actin in a distinct manner from rabbit muscle actin [13].

Other interactions of actin-binding

• The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins [14].
• TetraThymosinbeta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats [15].
• In these highly conserved genes, two previously known gene families have been brought together, families encoding the actin-binding proteins related to gelsolin and the leucine-rich-repeat (LRR) group of proteins involved in protein-protein interactions [7].
• The purified actin was highly pure and free of several known actin-binding proteins [13].

References