Document Detail


Actin reorganization is required for the formation of polarized B cell receptor signalosomes in response to both soluble and membrane-associated antigens.
MedLine Citation:
PMID:  22387556     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
B cells encounter both soluble Ag (sAg) and membrane-associated Ag (mAg) in the secondary lymphoid tissue, yet how the physical form of Ag modulates B cell activation remains unclear. This study compares actin reorganization and its role in BCR signalosome formation in mAg- and sAg-stimulated B cells. Both mAg and sAg induce F-actin accumulation and actin polymerization at BCR microclusters and at the outer rim of BCR central clusters, but the kinetics and magnitude of F-actin accumulation in mAg-stimulated B cells are greater than those in sAg-stimulated B cells. Accordingly, the actin regulatory factors, cofilin and gelsolin, are recruited to BCR clusters in both mAg- and sAg-stimulated B cells but with different kinetics and patterns of cellular redistribution. Inhibition of actin reorganization by stabilizing F-actin inhibits BCR clustering and tyrosine phosphorylation induced by both forms of Ag. Depolymerization of F-actin leads to unpolarized microclustering of BCRs and tyrosine phosphorylation in BCR microclusters without mAg and sAg, but with much slower kinetics than those induced by Ag. Therefore, actin reorganization, mediated via both polymerization and depolymerization, is required for the formation of BCR signalosomes in response to both mAg and sAg.
Authors:
Chaohong Liu; Heather Miller; Gregory Orlowski; Haiyin Hang; Arpita Upadhyaya; Wenxia Song
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-03-02
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  188     ISSN:  1550-6606     ISO Abbreviation:  J. Immunol.     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-03-23     Completed Date:  2012-06-04     Revised Date:  2014-09-10    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3237-46     Citation Subset:  AIM; IM    
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MeSH Terms
Descriptor/Qualifier:
Actin Cytoskeleton / ultrastructure*
Actin Depolymerizing Factors / physiology
Actins / chemistry*
Animals
Antigens / immunology*
Biopolymers
Cell Membrane / immunology
Cell Polarity
Cytoskeleton / ultrastructure*
Gelsolin / physiology
Lymphocyte Activation / immunology*
Mice
Mice, Inbred CBA
Phosphorylation
Protein Processing, Post-Translational
Protein Structure, Quaternary
Receptors, Antigen, B-Cell / immunology*
Solubility
Grant Support
ID/Acronym/Agency:
AI059617/AI/NIAID NIH HHS; R01 AI059617/AI/NIAID NIH HHS; R01 AI059617-01A2/AI/NIAID NIH HHS; R01 AI059617-02/AI/NIAID NIH HHS; R01 AI059617-03/AI/NIAID NIH HHS; R01 AI059617-04/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Actin Depolymerizing Factors; 0/Actins; 0/Antigens; 0/Biopolymers; 0/Gelsolin; 0/Receptors, Antigen, B-Cell
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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