Dynamic remodeling of the actin cytoskeleton by FMNL1γ is required for structural maintenance of the Golgi complex

Jessica M. Colón-Franco, Timothy S. Gomez, Daniel D Billadeau

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Formin-like 1 (FMNL1) is a member of the formin family of actin nucleators, and is one of the few formins for which in vitro activities have been well characterized. However, the functional roles of this mammalian formin remain ill-defined. In particular, it is unclear how the unique in vitro biochemical properties of FMNL1 relate to its regulation of cellular processes. Here, we demonstrate that FMNL1 depletion caused a dramatic increase in cellular F-actin content, which resulted in Golgi complex fragmentation. Moreover, increased Factin and maintenance of Golgi structure were distinctly regulated by the gamma isoform of FMNL1, which required binding to actin. Importantly, in addition to Golgi fragmentation, increased F-actin content in the absence of FMNL1 also led to cation-independent mannose 6-phosphate receptor dispersal, lysosomal enlargement and missorting of cathepsin D. Taken together, our data support a model in which FMNL1 regulates cellular F-actin levels required to maintain structural integrity of the Golgi complex and lysosomes.

Original languageEnglish (US)
Pages (from-to)3118-3126
Number of pages9
JournalJournal of Cell Science
Volume124
Issue number18
DOIs
StatePublished - Sep 15 2011

Fingerprint

Golgi Apparatus
Actin Cytoskeleton
Maintenance
Actins
IGF Type 2 Receptor
Cathepsin D
Lysosomes
formin 1
Cations
Protein Isoforms

Keywords

  • Actin
  • Formin proteins
  • Golgi complex

ASJC Scopus subject areas

  • Cell Biology

Cite this

Dynamic remodeling of the actin cytoskeleton by FMNL1γ is required for structural maintenance of the Golgi complex. / Colón-Franco, Jessica M.; Gomez, Timothy S.; Billadeau, Daniel D.

In: Journal of Cell Science, Vol. 124, No. 18, 15.09.2011, p. 3118-3126.

Research output: Contribution to journalArticle

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