Study 13 of 28DSIP literatureScience (New York, N.Y.)Top journal2026

An adaptor for feedback regulation of heme biosynthesis by a mitochondrial protease.

Not reported in abstract.

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Where it sits

this study against the rest of the dsip corpus

Preclinical · this one

Observational

Open-label

Randomised

Reviews

Summary and findings

Not reported in abstract.

How much of this paper we could read: title only (0.10). The feed gave us little more than the title, so our summary is thin. This says nothing about the study's quality — read the source. What this means →

2026

Abstract

The authors’ words, as Science (New York, N.Y.) supplied them

Heme biosynthesis is tightly coordinated to support essential functions without accumulating toxic porphyrins and depleting cellular iron. Heme induces degradation of the heme biosynthetic enzyme, 5-aminolevulinate synthase (ALAS), by the mitochondrial caseinolytic protease complex CLPX-CLPP (CLPXP), but the mechanism for heme-triggered degradation had not been elucidated. We found that polymerase delta-interacting protein 2 (POLDIP2) is a heme-sensing adaptor protein sufficient to reconstitute negative feedback degradation of ALAS by CLPXP. POLDIP2 was necessary to support ALAS turnover in cells and regulate heme production during erythropoiesis. POLDIP2 directly recognized and recruited heme-bound ALAS to CLPXP. Degradation initiation required a carboxyl-terminal element of ALAS, truncations of which cause an erythropoietic protoporphyria. Our findings establish a mechanism for conditional degradation by CLPXP that underlies erythropoietic protoporphyrias linked to CLPX and ALAS.

Background

Not reported in abstract.

Methods

Not reported in abstract.

Results

Not reported in abstract.

Interpretation

Not reported in abstract.

Limitations

Not reported in abstract.

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