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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2001-1-4
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nocodazole,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRIP10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin,
http://linkedlifedata.com/resource/pubmed/chemical/Vinculin,
http://linkedlifedata.com/resource/pubmed/chemical/WAS protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartyl-serine,
http://linkedlifedata.com/resource/pubmed/chemical/proto-oncogene protein c-fes-fps
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
113 Pt 23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4165-76
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11069762-Actin Cytoskeleton,
pubmed-meshheading:11069762-Actins,
pubmed-meshheading:11069762-Antineoplastic Agents,
pubmed-meshheading:11069762-Cell Adhesion,
pubmed-meshheading:11069762-Focal Adhesions,
pubmed-meshheading:11069762-Humans,
pubmed-meshheading:11069762-Macrophages,
pubmed-meshheading:11069762-Microinjections,
pubmed-meshheading:11069762-Microtubule-Associated Proteins,
pubmed-meshheading:11069762-Microtubules,
pubmed-meshheading:11069762-Mutagenesis,
pubmed-meshheading:11069762-Nocodazole,
pubmed-meshheading:11069762-Oligopeptides,
pubmed-meshheading:11069762-Peptide Fragments,
pubmed-meshheading:11069762-Protein Structure, Tertiary,
pubmed-meshheading:11069762-Protein-Tyrosine Kinases,
pubmed-meshheading:11069762-Proteins,
pubmed-meshheading:11069762-Proto-Oncogene Proteins,
pubmed-meshheading:11069762-Tubulin,
pubmed-meshheading:11069762-Vinculin,
pubmed-meshheading:11069762-Wiskott-Aldrich Syndrome Protein,
pubmed-meshheading:11069762-src Homology Domains
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pubmed:year |
2000
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pubmed:articleTitle |
Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages.
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pubmed:affiliation |
Institut für Prophylaxe und Epidemiologie der Kreislaufkrankheiten, Pettenkoferstr. 9, Germany. stefan.linder@klp.med.uni-muenchen.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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