Background

Antibodies to Proteins involved in Autophagy

• ATG16L1, Autophagy-related protein 16-1 (APG16-like 1)
  Homooligomer. Interacts with ATG5.
• AMBRA1, Activating molecule in BECN1-regulated autophagy protein 1
  Regulates autophagy and development of the nervous system. Involved in autophagy in controlling protein turnover during neuronal development, and in regulating normal cell survival and proliferation.
• ATG10, Ubiquitin-like-conjugating enzyme ATG10 (EC 6.3.2.-) (Autophagy-related protein 10) (APG10-like)
  E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for autophagy. Likely serves as an ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3.
• ATG12, Ubiquitin-like protein ATG12 (Autophagy-related protein 12) (APG12-like)
  Ubiquitin-like protein required for autophagy. Conjugated to ATG3 and ATG5.
• ATG3, Ubiquitin-like-conjugating enzyme ATG3 (EC 6.3.2.-) (Autophagy-related protein 3) (APG3-like) (hApg3) (Protein PC3-96)
  E2-like enzyme involved in autophagy and mitochondrial homeostasis. Catalyzes the conjugation of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to phosphatidylethanolamine (PE). PE-conjugation to ATG8-like proteins is essential for autophagy. Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3.
• ATG4A, Cysteine protease ATG4A (EC 3.4.22.-) (AUT-like 2 cysteine endopeptidase) (Autophagin-2) (Autophagy-related cysteine endopeptidase 2) (Autophagy-related protein 4 homolog A) (hAPG4A)
  Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP.
• ATG4B, Cysteine protease ATG4B (EC 3.4.22.-) (AUT-like 1 cysteine endopeptidase) (Autophagin-1) (Autophagy-related cysteine endopeptidase 1) (Autophagy-related protein 4 homolog B) (hAPG4B)
  Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.
• ATG4C, Cysteine protease ATG4C (EC 3.4.22.-) (AUT-like 3 cysteine endopeptidase) (Autophagin-3) (Autophagy-related cysteine endopeptidase 3) (Autophagy-related protein 4 homolog C)
  Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.
• ATG4D, Cysteine protease ATG4D (EC 3.4.22.-) (AUT-like 4 cysteine endopeptidase) (Autophagin-4) (Autophagy-related cysteine endopeptidase 4) (Autophagy-related protein 4 homolog D)
  Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.
• ATG5, Autophagy protein 5 (APG5-like) (Apoptosis-specific protein)
  Required for autophagy. Conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity.
• ATG7, Ubiquitin-like modifier-activating enzyme ATG7 (ATG12-activating enzyme E1 ATG7) (Autophagy-related protein 7) (APG7-like) (hAGP7) (Ubiquitin-activating enzyme E1-like protein)
  Functions as an E1 enzyme essential for multisubstrates such as ATG8-like proteins and ATG12. Forms intermediate conjugates with ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). PE-conjugation to ATG8-like proteins is essential for autophagy. Also acts as an E1 enzyme for ATG12 conjugation to ATG5 and ATG3.
• ATG9A, Autophagy-related protein 9A (APG9-like 1) (mATG9)
  Plays a role in autophagy. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and FAM48A.
• ATG14, Beclin 1-associated autophagy-related key regulator (Barkor) (Autophagy-related protein 14-like protein) (Atg14L)
  Required for both basal and inducible autophagy. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner.
• BECN1, Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) (Protein GT197)
  Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.
• DRAM1, DNA damage-regulated autophagy modulator protein 1 (Damage-regulated autophagy modulator)
  Lysosomal modulator of autophagy that plays a central role in p53/TP53-mediated apoptosis. Not involved in p73/TP73-mediated autophagy.
• HDAC6, Histone deacetylase 6 (HD6) (EC 3.5.1.98)
  Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degradated by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.
• MAP1LC3A, Microtubule-associated proteins 1A/1B light chain 3A (Autophagy-related protein LC3 A) (Autophagy-related ubiquitin-like modifier LC3 A) (MAP1 light chain 3-like protein 1) (MAP1A/MAP1B light chain 3 A) (MAP1A/MAP1B LC3 A) (Microtubule-associated protein 1 light chain 3 alpha)
  Probably involved in formation of autophagosomal vacuoles (autophagosomes).
• MAP1LC3B, Microtubule-associated proteins 1A/1B light chain 3B (Autophagy-related protein LC3 B) (Autophagy-related ubiquitin-like modifier LC3 B) (MAP1 light chain 3-like protein 2) (MAP1A/MAP1B light chain 3 B) (MAP1A/MAP1B LC3 B) (Microtubule-associated protein 1 light chain 3 beta)
  Probably involved in formation of autophagosomal vacuoles (autophagosomes).
• MAP1LC3C, Microtubule-associated proteins 1A/1B light chain 3C (Autophagy-related protein LC3 C) (Autophagy-related ubiquitin-like modifier LC3 C) (MAP1 light chain 3-like protein 3) (MAP1A/MAP1B light chain 3 C) (MAP1A/MAP1B LC3 C) (Microtubule-associated protein 1 light chain 3 gamma)
  Probably involved in formation of autophagosomal vacuoles (autophagosomes)
• PARK7, Protein DJ-1 (EC 3.4.-.-) (Oncogene DJ1) (Parkinson disease protein 7)
  Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.
• PINK1, Serine/threonine-protein kinase PINK1, mitochondrial (EC 2.7.11.1) (BRPK) (PTEN-induced putative kinase protein 1)
  Protects against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). It is necessary for PARK2 recruitement to dysfunctional mitochondria to initiate their degradation.
• PARK2, E3 ubiquitin-protein ligase parkin (EC 6.3.2.-) (Parkinson juvenile disease protein 2) (Parkinson disease protein 2)
  Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, ZNF746 and AIMP2. Mediates monoubiquitination as well as Lys-48-linked and Lys-63-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating Lys-63-linked polyubiquitination of misfolded proteins such as PARK7: Lys-63-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates Lys-63-linked polyubiquitination of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria. Mediates Lys-48-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in role in regulation of neuron death. Limits the production of reactive oxygen species (ROS). Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin-E during neuronal apoptosis. May represent a tumor suppressor gene.
• RAB24, Ras-related protein Rab-24
  May be involved in autophagy-related processes.
• RB1CC1, RB1-inducible coiled-coil protein 1
  Implicated in the regulation of RB1 expression. Functions as a DNA-binding transcription factor. Is a potent regulator of the RB1 pathway and a mediator that plays a crucial role in muscular differentiation. Expression is, thus, a prerequisite for myogenic differentiation. Involved in autophagy. Required for autophagosome formation.
• RGS19, Regulator of G-protein signaling 19 (RGS19) (G-alpha-interacting protein) (GAIP)
  Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein.
• KIAA0226, Run domain Beclin-1 interacting and cystein-rich containing protein (Rubicon) (Beclin-1 associated RUN domain containing protein) (Baron)
  Negatively regulates endocytic trafficking. Impairs the autophagosome maturation process. May inhibit PIK3C3 activity.
• ULK1, Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Unc-51-like kinase 1)
  Involved in autophagy. Required for autophagosome formation. Target of the TOR kinase signaling pathway that regulates autophagy through the control of phosphorylation status of ATG13/KIAA0652 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Phosphorylates ATG13/KIAA0652. Involved in axon growth. Plays an essential role in neurite extension of cerebellar granule cells.
• WIPI1, WD repeat domain phosphoinositide-interacting protein 1 (WIPI-1) (Atg18 protein homolog) (WD40 repeat protein interacting with phosphoinositides of 49 kDa) (WIPI 49 kDa)
  May play a role in autophagy. May regulate the trafficking of proteins involved in the mannose-6-phosphate receptor (MPR) recycling pathway.

References