ATP binding by NLRP7 is required for inflammasome activation in response to bacterial lipopeptides
详细信息 查看全文
- 作者：Alexander D. Radiana ; b ; Sonal Kharea ; Lan H. Chua ; b ; Andrea Dorfleutnera ; a-dorfleutner@northwestern.edu" class="auth_mail" title="E-mail the corresponding author ; Christian Stehlika ; c ; c-stehlik@northwestern.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：acLP ; acetylated lipopeptides ; ASC ; apoptosis-associated speck-like protein containing a CARD ; ATPase ; adenosine triphosphatases ; CARD ; caspase recruitment domain ; DAMP ; damage associated molecular pattern ; FLICA ; fluorescent labeled inhibitor of caspase-1 assay ; HEK293 ; human embryonic kidney 293 cells ; HKAL ; heat killed Acholeplasma laidlawii ; HM ; hydatidiform moles ; IL-1β ; interleukin-1β ; LRR ; leucine rich repeat ; NACHT ; NAIP ; CIITAHET-E and TP1 ; NAD ; NACHT associated domain ; NBD ; nucleotide
- 刊名：Molecular Immunology
- 出版年：2015
- 出版时间：October 2015
- 年：2015
- 卷：67
- 期：2
- 页码：294-302
- 全文大小：925 K
文摘
- class="listitem" id="list_lis0005">
- class="label">•
NLRP7 self-associates through its central nucleotide binding domain.
- class="label">•
NLRP7 binds ATP and exhibits ATPase activity.
- class="label">•
Disruption of the nucleotide binding Walker A motif results in loss of ATP binding.
- class="label">•
NLRP7 self-association and oligomerization are ATP dependent.
- class="label">•
NLRP7 inflammasome activation requires an intact nucleotide binding Walker A motif.