Work

Investigating The Enzymatic Redox Activity of Human Phosducin-Like Protein 2A

Year: 2025

Type: conference-paper

Abstract: Phosducin-like proteins (PhLPs) are a subclass of the thioredoxin (Trx) superfamily of proteins. The CryoEM structure of the chaperonin TriC/CCT complexed with PhLP2A supports the hypothesis that PhLPs are involved in the folding of cytoskeletal proteins, actin, and tubulin. However, the precise function of PhLP is not well understood. Several members of the Trx family of proteins are redox active and act as chaperones to assist protein folding. Additionally, the amino acid sequence alignment between TXNDC9 and PhLP2A reveals the redox-active cysteine to be conserved. We hypothesize that PhLP2A, like its structural homolog TXNDC9, is redox active.

Source: Loyola eCommons (Loyola University of Chicago)

Author: Tyszkowska, Sara

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W7057368168

FWCI:

Cites:

Cited by:

Related to: