Current Drug Targets
Isabel de Lavera, Ana Delgado Pavón, Marina Villanueva Paz, Manuel Oropesa-Ávila, Mario de la
Mata, Elizabet Alcocer-Gómez, Juan Garrido-Maraver, David Cotán, Mónica Álvarez-Córdoba and
José A. Sánchez-Alcázar
*
Centro Andaluz de Biología del Desarrollo [CABD], and Centro de Investigación Biomédica en Red: Enfermedades
Raras, Instituto de Salud Carlos III, Universidad Pablo de Olavide-Consejo Superior de Investigaciones Científicas,
Sevilla 41013, Spain
A R T I C L E H I S T O R Y
Received: February 22, 2016
Revised: April 20, 2016
Accepted: April 21, 2016
DOI:
10.2174/1389450117666160527143143
Abstract: Background: The molecular crosstalk between inflammation and autophagy is an emerg-
ing field of research that is essential for the understanding of multicellular organism homeostasis and
how these processes influence a variety of pathological conditions.
Objective: In this review, we briefly describe the relationship between autophagy and inflammasome
activation. The central role that mitochondria play in both cellular processes is also discussed.
Conclusion: Inflammasome and autophagy often modulate each other by common inhibitory mecha-
nisms that are controlled by different input pathways. Thus, inflammasome components coordinate
autophagy and autophagy regulates inflammasome activation, making the balance between both proc-
esses a fundamental player in cellular homeostasis.
Keywords: Autophagy, cytokines, inflammasome, mitochondria, NLRP3, ROS.
1. INFLAMMASOME AND INFLAMMASOME TYPES
Multicellular organisms have developed molecular sen-
sors to detect pathogens and damaging molecules by intra-
cellular receptors, termed pattern recognition receptors
(PRRs). PRRs sense pathogen associated molecular patterns
(PAMPs) or damage associated molecular patterns (DAMPs)
[1, 2]. After detection, PRRs activate the proper defense
pathways to preserve cell survival.
Four different families of PRRs have been described: C-
type lectin receptors (CLRs), retinoic acid-inducible gene
(RIG)-I-like receptors (RLRs), Toll-like receptors (TLRs),
and nucleotide binding and oligomerization domain (NOD)-
like receptors (NLRs), for a complete description, see [3]. In
this review we will focus on NLRs, the so-called “inflamma-
somes”, the prototypic pathogen/danger-sensing receptors
that was first described in detail in 2002 [4]. NLRs are a
family of proteins codified by at least 23 human genes re-
sponsible for sensing pathogens and damaging molecules
[5]. This family of receptors is present in mammals, plants
and invertebrates and its structure and function have been
extensively studied in mammals [6].
Inflammasome is a cytosolic multiprotein intracellular
signaling complex assembled as a consequence of infection,
*Address correspondence to this author at the Centro Andaluz de Biología
del Desarrollo [CABD]. Universidad Pablo de Olavide-Consejo Superior de
Investigaciones Científicas. Carretera de Utrera Km 1, Sevilla 41013, Spain;
Tel: 34 954978071; Fax: 34 954349376; E-mail: jasanalc@upo.es.
environmental stress or cell damage that participates in the
production of pro-inflammatory interleukins (IL) such as IL-
1β and IL-18 and the regulation of the inflammation re-
sponse [7, 8]. Additionally to the maturation of pro-
inflammatory cytokines, the inflammasome complexes may
target different signaling pathways regulating diverse
physiological functions such as tissue repair and cell death
by pyroptosis [9].
Numerous inflammasomes have been identified so far,
including NLRs such as NLRP1, NLRP2, NLRP3, NLRC4
and double-stranded DNA (dsDNA) sensors absent in mela-
noma 2 [AIM2] and interferon-inducible protein-16 (IFI-16)
[10, 11]. AIM2 and interferon-inducible protein-16 (IFI-16)
are structurally different to the other NLRs, although they
are functionally related.
The mechanisms of activation of the different types of in-
flammasomes have been recently reviewed [12]. Most
NLRPs have a common molecular organization formed by
three main functional domains: an Nterminal CARD or
PYRIN (PYD) protein interaction domain; a central nucleo-
tide-binding domain [NBD] for oligomerisation; and C-
terminal leucine-rich repeats (LRRs), for pathogen sensing
[13]. AIM2 and IFI16 belonging to the PYHIN (PYD and
HIN domain-containing proteins) family. AIM2 has one
DNA-binding HIN domain for detecting nucleic acids, and a
PYD domain to interact with ASC [14]. IFI16 has one PYD
and two HIN domains, and signals through STING [for
stimulator of interferon genes] to regulate type I IFN re-
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1030
Current Drug Targets, 2017, 18, 1030-1038
REVIEW ARTICLE
The Connections Among Autophagy, Inflammasome and Mitochondria