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Article

Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function.

Current biology : CB - 21 Jun 2005

Gangar Akanksha, Rossi Guendalina, Andreeva Anna, Hales Robert, Brennwald Patrick

Abstract excerpt

The Lethal giant larvae (Lgl) tumor suppressor family is conserved from yeast to mammals and plays a critical yet controversial role in cell polarity. Studies on Drosophila Lgl suggest that its function in polarity is through regulation of the acto-myosin cytoskeleton. In contrast, studies on the...

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Source

Identifiers

PMID: 15964280
DOI: 10.1016/j.cub.2005.05.046

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-15964280-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function.PMID 15964280Read ↗

Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis.Semantic proximity Read ↗

Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis.Semantic proximity Read ↗

Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9.Semantic proximity Read ↗

Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function.Semantic proximity Read ↗

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