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PMID: 11069762 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages.

Journal of cell science ·Vol. 113 Pt 23 ·2000-12-00 ·Pages 4165-76

Linder S, Hüfner K, Wintergerst U, Aepfelbacher M

Abstract

Podosomes are unique actin-rich adhesion structures of monocyte-derived cells such as macrophages and osteoclasts. They clearly differ from other substratum-contacting organelles like focal adhesions in morphological and functional regards. Formation of podosomes has been shown to be dependent on the small GTPase CDC42Hs and its effector Wiskott-Aldrich syndrome protein (WASp). In this study, we investigated the functional relation between podosomes and the microtubule system in primary human macrophages. We demonstrate that, in contrast to focal adhesions, assembly of podosomes in macrophages and their monocytic precursors is dependent on an intact microtubule system. In contrast, experiments using Wiskott-Aldrich syndrome (WAS) macrophages indicate that the microtubule system is not reciprocally dependent on podosomes. A potential linker between podosomes and microtubules may be WASp itself, considering that microinjection of the WASp polyproline domain prevents podosome reassembly. This polyproline domain is thought to link WASp to microtubules via CDC42 interacting protein 4 (CIP4). Consistently, macrophages microinjected with CIP4 constructs deficient in either the microtubule- or the WASp-binding domain also fail to reassemble podosomes. In sum, our findings show that microtubules are essential for podosome formation in primary human macrophages and that WASp and CIP4 may be involved in this phenomenon.

MeSH Terms
Actin Cytoskeleton/metabolism Actins/analysis Antineoplastic Agents/pharmacology Cell Adhesion/drug effects,physiology Focal Adhesions/drug effects,metabolism Humans Macrophages/chemistry,physiology,ultrastructure Microinjections Microtubule-Associated Proteins/metabolism Microtubules/metabolism Minor Histocompatibility Antigens Mutagenesis/physiology Nocodazole/pharmacology Oligopeptides/metabolism,pharmacology Peptide Fragments/metabolism,pharmacology Protein Structure, Tertiary Protein-Tyrosine Kinases Proteins/chemistry,metabolism,pharmacology Proto-Oncogene Proteins/chemistry,genetics Tubulin/analysis Vinculin/analysis Wiskott-Aldrich Syndrome Protein src Homology Domains/genetics
Chemicals
Actins Antineoplastic Agents Microtubule-Associated Proteins Minor Histocompatibility Antigens Oligopeptides Peptide Fragments Proteins Proto-Oncogene Proteins TRIP10 protein, human Tubulin WAS protein, human Wiskott-Aldrich Syndrome Protein proto-oncogene protein c-fes-fps Vinculin arginyl-glycyl-aspartyl-serine Protein-Tyrosine Kinases Nocodazole
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Linder S
Institut für Prophylaxe und Epidemiologie der Kreislaufkrankheiten, Pettenkoferstr. 9, Germany. stefan.linder@klp.med.uni-muenchen.de
Hüfner K
Wintergerst U
Aepfelbacher M
Article Info
Journal
Journal of cell science
Abbr.
J Cell Sci
ISSN
0021-9533
Published
2000-12-00
Pages
4165-76
Language
English
Region
England
NLM ID
0052457
Subset
IM
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