| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Kung, Sam K. P. Yan, Qi Yang, Tao Yoshioka, Katsuji Cheng, Hui Du, Juan Wang, Hui-ming Ding, Guo-hua |
| Description |
Author Affiliation: Wang HM ( From the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China, wanghuimingwhm@yahoo.com.); Yan Q ( From the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.); Yang T ( From the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.); Cheng H ( From the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.); Du J ( From the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China.); Yoshioka K ( the Division of Molecular Cell Signaling, Department of Molecular and Cellular Biology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan.); Kung SK ( the Department of Immunology, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada, and.); Ding GH ( From the Department of Nephrology, Renmin Hospital of Wuhan University, Wuhan 430060, China, ghxding@gmail.com.) |
| Abstract |
CD40 expression on the surface of B lymphocytes is essential for their biological function and fate decision. The engagement of CD40 with its cognate ligand, CD154, leads to a sequence of cellular events in B lymphocytes, including CD40 cytoplasmic translocation, a temporal and spatial organization of effector molecules, and a cascade of CD40-induced signal transduction. The JLP scaffold protein was expressed in murine B lymphocytes. Using B lymphocytes from jlp-deficient mice, we observed that JLP deficiency resulted in defective CD40 internalization upon CD154/CD40 engagement. Examination of interactions and co-localization among CD40, JLP, dynein, and Rab5 in B lymphocytes suggested that CD40 internalization is a process of JLP-mediated vesicle transportation that depends on Rab5 and dynein. JLP deficiency also diminished CD40-dependent activation of MAPK and JNK, but not NF-κB. Inhibiting vesicle transportation from the direction of cell periphery to the cell center by a dynein inhibitor (ciliobrevin D) impaired both CD154-induced CD40 internalization and CD40-dependent MAPK activities in B lymphocytes. Collectively, our data demonstrate a novel role of the JLP scaffold protein in the bridging of CD154-triggered CD40 internalization and CD40-dependent signaling in splenic B lymphocytes. |
| ISSN |
00219258 |
| e-ISSN |
1083351X |
| Journal |
Journal of Biological Chemistry |
| Issue Number |
9 |
| Volume Number |
290 |
| Language |
English |
| Publisher |
American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date |
2015-02-27 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Adaptor Proteins, Signal Transducing Metabolism Antigens, CD40 B-Lymphocytes Signal Transduction Deficiency Genetics Animals Blotting, Western CD40 Ligand Cells, Cultured Dyneins Endocytosis Flow Cytometry HEK293 Cells JNK Mitogen-Activated Protein Kinases Mice, Knockout Microscopy, Confocal Mitogen-Activated Protein Kinases Protein Binding RNA Interference Spleen Cytology Rab5 GTP-Binding Proteins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Cell Biology Biochemistry Molecular Biology |
