Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles

Kirsten Heimann, Justin M. Percival, Ron Weinberger, Peter Gunning, Jennifer L. Stow

Research output: Contribution to journalArticlepeer-review

98 Scopus citations


Golgi membranes and Golgi-derived vesicles are associated with multiple cytoskeletal proteins and motors, the diversity and distribution of which have not yet been defined. Carrier vesicles were separated from Golgi membranes, using an in vitro budding assay, and different populations of vesicles were separated using sucrose density gradients. Three main populations of vesicles labeled with β-COP, γ-adaptin, or p200/myosin II were separated and analyzed for the presence of actin/actin-binding proteins. β-Actin was bound to Golgi cisternae and to all populations of newly budded vesicles. Centractin was selectively associated with vesicles co-distributing with β-COP-vesicles, while p200/myosin II (non-muscle myosin IIA) and non- muscle myosin IIB were found on different vesicle populations. Isoforms of the Tm5 tropomyosins were found on selected Golgi-derived vesicles, while other Tm isoforms did not colocalize with Tm5 indicating the association of specialized actin filaments with Golgi-derived vesicles. Golgi-derived vesicles were shown to bind to F-actin polymerized from cytosol with Jasplakinolide. Thus, newly budded, coated vesicles derived from Golgi membranes can bind to actin and are customized for differential interactions with microfilaments by the presence of selective arrays of actin-binding proteins.

Original languageEnglish (US)
Pages (from-to)10743-10750
Number of pages8
JournalJournal of Biological Chemistry
Issue number16
StatePublished - Apr 16 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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