Proteomics

Dataset Information

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IP-MS of ALS-linked PFN1 variants

ABSTRACT: Dominant mutations in profilin-1 (PFN1) are associated with amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease characterized by motor neuron loss, paralysis, and death from respiratory failure. Our lab recently demonstrated that PFN1 mutant proteins are destabilized—they unfold at milder conditions during thermal and chemical denaturation. Furthermore, we and others have shown that mutant PFN1 is more prone to misfold and aggregate. This misfolding alters the protein-protein interactions of PFN1, as demonstrated by an immunoprecipitation-mass spectrometry (IP-MS) screen of wild-type and ALS-associated PFN1 variants. While ALS-associated mutants do not show loss of interaction, several variants have altered interactions with one or several formin family proteins, a group of proteins that interact with profilins to regulate actin polymerization.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

DISEASE(S): Amyotrophic Lateral Sclerosis

SUBMITTER: Daryl Bosco  

LAB HEAD: Daryl Bosco

PROVIDER: PXD015602 | Pride | 2022-02-15

REPOSITORIES: pride

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090817CG.msf Msf
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Publications

ALS-linked PFN1 variants exhibit loss and gain of functions in the context of formin-induced actin polymerization.

Schmidt Eric J EJ   Funes Salome S   McKeon Jeanne E JE   Morgan Brittany R BR   Boopathy Sivakumar S   O'Connor Lauren C LC   Bilsel Osman O   Massi Francesca F   Jégou Antoine A   Bosco Daryl A DA  

Proceedings of the National Academy of Sciences of the United States of America 20210601 23

Profilin-1 (PFN1) plays important roles in modulating actin dynamics through binding both monomeric actin and proteins enriched with polyproline motifs. Mutations in PFN1 have been linked to the neurodegenerative disease amyotrophic lateral sclerosis (ALS). However, whether ALS-linked mutations affect PFN1 function has remained unclear. To address this question, we employed an unbiased proteomics analysis in mammalian cells to identify proteins that differentially interact with mutant and wild-t  ...[more]

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