Oligomerized CARD16 promotes caspase-1 assembly and IL-1β processing
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- 作者：Tadayoshi Karasawaa ; tdys.karasawa@jichi.ac.jp" class="auth_mail" title="E-mail the corresponding author ; Akira Kawashimaa ; Fumitake Usuia ; Hiroaki Kimuraa ; Koumei Shirasunaa ; Yoshiyuki Inouea ; Takanori Komadaa ; Motoi Kobayashia ; Yoshiko Mizushinaa ; Junji Sagarab ; Masafumi Takahashia ; masafumi2@jichi.ac.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：ANOVA ; analysis of variance ; ASC ; apoptosis-associated speck-like protein containing a caspase recruitment domain ; Bcl10 ; B-cell lymphoma/leukemia 10 ; BS3 ; bis(sulfosccinimidyl)suberate ; CARD ; caspase recruitment domain ; CARMA1 ; CARD-membrane-associated guanylate kinase 1 ; COPs ; CARD-only proteins ; CASP1 ; caspase-1 ; ELISA ; enzyme-linked immunosorbent assay ; FCS ; fetal calf serum ; IL ; interleukin ; LPS ; lipopolysaccharide ; LRRs ; leucine-rich repeats ; NLRs ; nucleotide-binding domain leucine-rich re
- 刊名：FEBS Open Bio
- 出版年：2015
- 出版时间：2015
- 年：2015
- 卷：5
- 期：Complete
- 页码：348-356
- 全文大小：2644 K
文摘
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CARD16 is the most abundant CARD-only protein in hematopoietic cells.
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Unlike CARD17, CARD16 oligomerizes to form a filament-like structure.
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The filament-like structure formed by CARD16 promotes caspase 1 (CASP1) assembly.
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CASP1-dependent IL-1β processing is enhanced by CARD16.
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CARD16 colocalizes in ASC-speck by interacting with ASC.
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