Phosducin-like protein 3 (PhLP3)

Phosducin-like protein 3 (PhLP3) is a member of the phosducin-like protein family, which are small cytosolic proteins that function primarily as molecular chaperones or co-chaperones. Unlike PhLP1, PhLP3 does not play a major role in G protein signaling but instead assists the cytosolic chaperonin complex (CCT) in the folding of β-tubulin and possibly actin, thus regulating cytoskeletal dynamics[1][2][4]. PhLP3 contains a conserved thioredoxin domain and exhibits redox activity, although it does not have a canonical CXXC motif[2]. In yeast and protozoan systems, PhLP3 is essential for proper β-tubulin folding, with genetic deletion protecting cells from free β-tubulin toxicity and knockdown causing defects in microtubule architecture[1][2]. While PhLP3 is highly conserved across eukaryotes, there is limited evidence that it is a direct therapeutic target or that it plays a well-defined role in human disease[1][2][4].

Other names

Phosducin-like 3PhLP-3PLP3