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Article

How lamina-associated polypeptide 1 (LAP1) activates Torsin.

eLife - 22 Aug 2014

Sosa Brian A, Demircioglu F Esra, Chen James Z, Ingram Jessica, Ploegh Hidde L, Schwartz Thomas U

Abstract excerpt

Lamina-associated polypeptide 1 (LAP1) resides at the nuclear envelope and interacts with Torsins, poorly understood endoplasmic reticulum (ER)-localized AAA+ ATPases, through a conserved, perinuclear domain. We determined the crystal structure of the perinuclear domain of human LAP1. LAP1 possesses an atypical AAA+ fold. While LAP1 lacks canonical nucleotide binding motifs, its strictly conserved arginine 563 is...

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Identifiers

PMID: 25149450
DOI: 10.7554/eLife.03239
PMCID: PMC4358337

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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How lamina-associated polypeptide 1 (LAP1) activates Torsin.PMID 25149450Read ↗

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