Disease relevance of Gel

• The recombinant lobster gelsolin-like protein, expressed in Escherichia coli as a fusion protein, was purified from inclusion bodies and renatured as a functional protein [1].

High impact information on Gel

• Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ [2].
• Coverslips coated with gelsolin, a multi-domain, calcium-dependent capping and severing protein, bound rhodamine-phalloidin-saturated filaments along their length in the presence of EGTA [2].
• DNA polymerase insertion fidelity. Gel assay for site-specific kinetics [3].
• We have analysed the developmental defects in Drosophila embryos lacking a gelsolin-related protein encoded by the gene flightless I [4].
• The cDNA contained an open reading frame of 2.265 kb, and the deduced amino acid sequence of 754 residues (83,469 Da) identified the protein as a cytoplasmic member of the gelsolin/villin protein family [1].

Biological context of Gel

• Comparison of the lobster gelsolin amino acid sequence with other members of this protein family revealed the characteristic 6-fold repeated segmental structure as well as the three conserved sequence motifs typical of each segment [Way and Weeds (1988) J. Mol. Biol. 203, 1127-1133] [1].
• A tail-muscle-specific cDNA library was constructed in a lambda expression vector and a full-length clone was obtained by screening with a polyclonal anti-(crustacean gelsolin) antibody [1].

Anatomical context of Gel

• One candidate for coupling membrane events to neurite retraction is the microfilament-associated protein gelsolin which, in its calcium-activated state, severs actin filaments [5].

Analytical, diagnostic and therapeutic context of Gel

• A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression [1].

References