Tax1-binding protein 1 is expressed in the retina and interacts with the GABAC receptor ρ1 subunit

Ulrich, Melanie; Seeber, Silke; Becker, Cord‐Michael; Enz, Ralf

doi:10.1042/bj20061036

Cited by 12 publications

(8 citation statements)

References 43 publications

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“…TAX protein is localized in the nucleus and cytoplasm of infected cells. There it interacts with different host proteins such as TAX1BP1 in order to regulate viral and cellular transcription, signal transduction pathways, and apoptosis [27]. This would explain the cytoplasmic and nuclear localization of TAX1BP1 in neurons (Fig 3).…”

Section: Discussionmentioning

confidence: 99%

Comparative distribution of protein components of the A20 ubiquitin-editing complex in normal human brain

Pranski

Sanford

Dalal

et al. 2012

Neuroscience Letters

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Activation of innate and adaptive immune responses is tightly regulated, as insufficient activation could result in defective clearance of pathogens, while excessive activation might lead to lethal systemic inflammation or autoimmunity. A20 functions as a negative regulator of innate and adaptive immunity by inhibiting NF-κB activation. A20 mediates its inhibitory function in a complex with other proteins including RNF11 and Itch, both E3 ubiquitin ligases and TAX1BP1, an adaptor protein. Since NF-κB has been strongly implicated in various neuronal functions, we predict that its inhibitor, the A20 complex, is also present in the nervous system. In efforts to better understand the role of A20 complex and NF-κB signaling pathway, we determined regional distribution of A20 mRNA as well as protein expression levels and distribution of RNF11, TAX1BP1 and Itch, in different brain regions. The distribution of TRAF6 was also investigated since TRAF6, also an E3 ligase, has an important role in NF-κB signaling pathway. Our investigations, for the first time, describe and demonstrate that the essential components of the A20 ubiquitin-editing complex are present and mainly expressed in neurons. The A20 complex components are also differentially expressed throughout the human brain. This study provides useful information about region specific expression of the A20 complex components that will be invaluable while determining the role of NF-κB signaling pathway in neuronal development and degeneration.

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Section: Discussionmentioning

confidence: 99%

Comparative distribution of protein components of the A20 ubiquitin-editing complex in normal human brain

Pranski

Sanford

Dalal

et al. 2012

Neuroscience Letters

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“…Besides those mentioned above, other TAX1BP1-interacting proteins include ubiquitin-like proteins of the LC3/GABARAP family (Newman et al, 2012), GABAC receptors 1 subunit (Ulrich et al, 2007), myosin VI (Morriswood et al, 2007), RhoGAP (Nagaraja & Kandpal, 2004), A20 binding inhibitor of NF-B (ABIN) 1 (Gao et al, 2011), optineurin (Journo et al, 2009), ring finger protein 11 (RNF11; Shembade et al, 2009) and itchy E3 ubiquitin protein ligase homolog (ITCH; Shembade et al, 2008). TAX1BP1 may also mediate the formation of multi-subunit protein complexes.…”

Section: Introductionmentioning

confidence: 98%

“…TAX1BP1 has also been implicated in some other functions, such as autophagy (Newman et al, 2012), membrane trafficking (Morriswood et al, 2007) and neurotransmission (Ulrich et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Expression, purification and crystallization of the SKICH domain of human TAX1BP1

et al. 2014

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TAX1BP1 is a highly conserved, pleiotropic protein that plays many essential functions in human cells, including negative regulation of inflammatory and antimicrobial responses mediated by NF-κB and IRF3 signaling, inhibition of apoptosis, transcriptional coactivation and autophagy etc. TAX1BP1 contains a SKICH domain at the N-terminus, three coiled-coil domains in the middle and two ubiquitin-binding zinc-finger motifs at the C-terminus. The SKICH domain and the linker sequence between the SKICH domain and the coiled-coil region mediate interaction with ubiquitin-like proteins of the LC3/GABARAP family, which are autophagosome markers. For structure determination of the SKICH domain of TAX1BP1, a protein construct (amino acids 15-148) corresponding to the SKICH domain plus the linker region was expressed, purified and crystallized. A native diffraction data set has been collected to 1.9 Å resolution. A molecular-replacement solution has been found by using the structure of the SKICH domain of NDP52, a paralog of TAX1BP1.

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“…Binding of Tax1 to TAX1BP1 disrupts TAX1BP1-A20 interaction and thus evokes constitutive activation of NF-κB (Shembade et al, 2008). TAX1BP1 also assumes functional roles in a number of other processes, including cell growth and apoptosis (De Valck et al, 1999;Matsusaka & Pines, 2004;Nagaraja & Kandpal, 2004), transcriptional coactivation (Chin, Chun, Ching, Jeang, & Jin, 2007;Wang, Naidu, Sverdrup, & Androphy, 2009), membrane trafficking (Morriswood et al, 2007), neurotransmission (Ulrich, Seeber, Becker, & Enz, 2007), and autophagy (Newman et al, 2012). The mechanisms for the involvement of TAX1BP1 in these processes are less well characterised and understood.…”

mentioning

confidence: 98%

“…Besides TAX1, A20, and the signalling molecules in the NF-κB and IRF3 pathways, other TAX1BP1 interacting proteins include: the LC3/GABARAP family of ubiquitin-like proteins (Newman et al, 2012), the ρ1 subunit of the GABAC receptors (Ulrich et al, 2007), myosin VI (Morriswood et al, 2007), RhoGAP (Nagaraja & Kandpal, 2004), A20 binding inhibitor of NF-κB (ABIN) 1 (Gao et al, 2011), Optineurin (Journo et al, 2009), ring finger protein 11 (RNF11) (Shembade et al, 2009) and itchy E3 ubiquitin protein ligase homolog (ITCH) (Shembade et al, 2008). The various functions of TAX1BP1 likely are dependent on the association of TAX1BP1 with different protein partners.…”

mentioning

confidence: 99%

Crystallographic and modelling studies suggest that the SKICH domains from different protein families share a common Ig-like fold but harbour substantial structural variations

Yang

Wang

Huang

et al. 2014

Journal of Biomolecular Structure and Dynamics

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TAX1BP1 is a pleiotropic multi-domain protein involved in many important biological processes such as signal transduction, cell growth and apoptosis, transcriptional coactivation, membrane trafficking, neurotransmission and autophagy. The N-terminus of TAX1BP1 contains a SKICH domain implicated in autophagy. SKICH domains are also present in four other proteins including NDP52, CALCOCO1, SKIP and PIPP. The SKICH domains of SKIP and PIPP mediate plasma membrane localisation. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known. Here we report the crystal structure of the TAX1BP1 SKICH domain, which has an Ig-like fold similar to the NDP52 SKICH domain. Extensive pairwise and clustered aromatic π-stacking interactions are present in the TAX1BP1 SKICH domain. The aromatic residues mediating these interactions can be classified into four groups with varying degrees of conservation among different protein families. The interactions mediated by highly conserved residues are found in the interior and one outward face of the Ig-like β-barrel, representing common structural features of the SKICH domains. Three TAX1BP1-specific pairwise interactions locate in the loop regions, each augmented by a proline-aromatic interaction. The three proline-aromatic clusters are linked together by more generic hydrophobic interactions, forming a unique hydrophobic surface at one end of the TAX1BP1 SKICH domain. The structures and homologous models of SKICH domains from different proteins reveal substantial differences in electrostatic surface properties of the domains. Together with existing biochemical data, results from the structural study suggest that an intact SKICH domain is required for the autophagy function of TAX1BP1.

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Tax1-binding protein 1 is expressed in the retina and interacts with the GABAC receptor ρ1 subunit

Cited by 12 publications

References 43 publications

Comparative distribution of protein components of the A20 ubiquitin-editing complex in normal human brain

Comparative distribution of protein components of the A20 ubiquitin-editing complex in normal human brain

Expression, purification and crystallization of the SKICH domain of human TAX1BP1

Crystallographic and modelling studies suggest that the SKICH domains from different protein families share a common Ig-like fold but harbour substantial structural variations

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