Abstract：
:The activated leukocyte cell adhesion molecule (ALCAM) is dynamically regulated by the actin cytoskeleton. In this study we explored the molecular mechanisms and signaling pathways underlying the cytoskeletal restraints of this homotypic adhesion molecule. We observed that ALCAM-mediated adhesion induced by cytoskeleton-disrupting agents is accompanied by activation of the small GTPases RhoA, Rac1 and Cdc42. Interestingly, unlike adhesion mediated by integrins or cadherins, ALCAM-mediated adhesion appears to be independent of Rho-like GTPase activity. By contrast, we demonstrated that protein kinase C (PKC) plays a major role in ALCAM-mediated adhesion. PKC inhibition by chelerythrine chloride and myristoylated PKC pseudosubstrate, as well as PKC downregulation by PMA strongly reduce cytoskeleton-dependent ALCAM-mediated adhesion. Since serine and threonine residues are dispensable for ALCAM-mediated adhesion and ALCAM is not phosphorylated, we can rule out that ALCAM itself is a direct PKC substrate. We conclude that PKCalpha plays a dominant role in cytoskeleton-dependent avidity modulation of ALCAM.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Zimmerman AW,Nelissen JM,van Emst-de Vries SE,Willems PH,de Lange F,Collard JG,van Leeuwen FN,Figdor CGdoi
10.1242/jcs.01139keywords:
subject
Has Abstractpub_date
2004-06-01 00:00:00pages
2841-52issue
Pt 13eissn
0021-9533issn
1477-9137pii
117/13/2841journal_volume
117pub_type
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pub_type： 评论,杂志文章,评审
doi：
更新日期：2001-10-01 00:00:00
