Molecular cloning, expression and regulation of the avian tubby-like protein 1 (tulp1) gene

Heikenwälder, Mathias; Koritschoner, Nicolás P.; Pajer, Petr; Chaboissier, Marie-Christine; Kurz, Steffen M; Briegel, Karoline J.; Bartůněk, Petr; Zenke, Martin

doi:10.1016/s0378-1119(01)00578-9

Cited by 18 publications

(8 citation statements)

References 25 publications

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“…Tubby-like proteins (TLPs) are present in all eukaryotes, from single-celled to multicellular organisms (Liu, 2008), including Caenorthabditis elegans, Drosophila, Arabidopsis , rice, maize, chicken, and mouse (North et al, 1997; Heikenwalder et al, 2001; Ronshaugen et al, 2002; Figlewicz et al, 2004). TLPs have a typical tubby domain that forms a closed β barrel with 12 anti-parallel strands and a central hydrophobic α helix (Boggon et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Expression Analysis of the Tubby-Like Protein Family in the Malus domestica Genome

Xing

Zhang

et al. 2016

Front. Plant Sci.

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Tubby-like proteins (TLPs), which have a highly conserved β barrel tubby domain, have been found to be associated with some animal-specific characteristics. In the plant kingdom, more than 10 TLP family members were identified in Arabidopsis, rice and maize, and they were found to be involved in responses to stress. The publication of the apple genome makes it feasible to systematically study the TLP family in apple. In this investigation, nine TLP encoding genes (TLPs for short) were identified. When combined with the TLPs from other plant species, the TLPs were divided into three groups (group A, B, and C). Most plant TLP members in group A contained an additional F-box domain at the N-terminus. However, no common domain was identified other than tubby domain either in group B or in group C. An analysis of the tubby domains of MdTLPs identified three types of conserved motifs. Motif 1 and 2, the signature motifs in the confirmed TLPs, were always present in MdTLPs, while motif 3 was absent from group B. Homology modeling indicated that the tubby domain of most MdTLPs had a closed β barrel, as in animal tubby domains. Expression profiling revealed that the MdTLP genes were expressed in multiple organs and were abundant in roots, stems, and leaves but low in flowers. An analysis of cis-acting elements showed that elements related to the stress response were prevalent in the promoter sequences of MdTLPs. Expression profiling by qRT-PCR indicated that almost all MdTLPs were up-regulated at some extent under abiotic stress, exogenous ABA and H2O2 treatments in leaves and roots, though different MdTLP members exhibited differently in leaves and roots. The results and information above may provide a basis for further investigation of TLP function in plants.

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Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Expression Analysis of the Tubby-Like Protein Family in the Malus domestica Genome

Xing

Zhang

et al. 2016

Front. Plant Sci.

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“…TUB is the founding-member of the tubby-like proteins and is conserved among vertebrate genomes (2). Interestingly, a loss of function mutation of tub results in the tubby mouse syndrome, which is characterized by late-onset obesity and neurosensory deficits.…”

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confidence: 99%

Identification of TUB as a Novel Candidate Gene Influencing Body Weight in Humans

et al. 2006

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Previously, we identified a locus on 11p influencing obesity in families with type 2 diabetes. Based on mouse studies, we selected TUB as a functional candidate gene and performed association studies to determine whether this controls obesity. We analyzed the genotypes of 13 single nucleotide polymorphisms (SNPs) around TUB in 492 unrelated type 2 diabetic patients with known BMI values. One SNP (rs1528133) was found to have a significant effect on BMI (1.54 kg/m 2 , P ‫؍‬ 0.006). This association was confirmed in a population enriched for type 2 diabetes, using 750 individuals who were not selected for type 2 diabetes. Two SNPs in linkage disequilibrium with rs1528133 and mapping to the 3 end of TUB, rs2272382, and rs2272383 also affected BMI by 1.3 kg/m2 (P ‫؍‬ 0.016 and P ‫؍‬ 0.010, respectively). Combined analysis confirmed this association (P ‫؍‬ 0.005 and P ‫؍‬ 0.002, respectively). Moreover, comparing 349 obese subjects (BMI >30 kg/m 2 ) from the combined cohort with 289 normal subjects (BMI <25 kg/m 2 ) revealed that the protective alleles have a lower frequency in obese subjects (odds ratio 1.32 [95% CI 1.04 -1.67], P ‫؍‬ 0.022). Altogether, data from the tubby mouse as well as these data suggest that TUB could be an important factor in controlling the central regulation of body weight in humans. Diabetes 55:385-389, 2006

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“…Tub encodes a highly hydrophilic protein containing putative tyrosine phosphorylation and Src homology 2 (SH2)-docking sites [8]. Phosphotyrosine-mediated interactions with SH2-containing signaling proteins have been shown to play an important role in intracellular signal transduction [9]. To date, however, many questions remain about the role of tubby and its signal pathway.…”

Section: Introductionmentioning

confidence: 99%

Insulin Phosphorylates Tyrosine Residue 464 of Tub and Translocates Tubby into the Nucleus in HIRcB Cells

Kim

et al. 2014

Endocrinol Metab

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BackgroundThe tubby protein has a motif that might be relevant for its action in the insulin signaling pathway. Previous studies have indicated that tubby undergoes phosphorylation on tyrosine residues in response to several stimuli and is known to localize in the nucleus as well as in the plasma membrane. However, the relationship between phosphorylation and nuclear translocation is not well understood. Here, we report that insulin directly phosphorylates tubby, which translocates into the nucleus.MethodsThe effects of insulin on Tubby were performed with Western blot. The immunoprecipitation and confocal microscopy were performed to prove phosphorylation and nuclear translocation.ResultsMutation study reveals that tyrosine residue 464 of tubby gene (Tub) is a phosphorylation site activated by insulin. In addition, major portions of tubby protein in the plasma membrane are translocated into the nucleus after insulin treatment. Tyrosine kinase inhibitor pretreatment blocked insulin-induced tubby translocation, suggesting that phosphorylation is important for nuclear translocation. Moreover, mutant tyrosine residue 464 did not translocate into the nucleus in respond to insulin. These findings demonstrate that insulin phosphorylates tyrosine residue 464 of Tub, and this event is important for insulin-induced tubby nuclear translocation.ConclusionInsulin phosphorylates tyrosine residue 464 of Tub and translocates tubby into the nuclei of HIRcB cells.

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Molecular cloning, expression and regulation of the avian tubby-like protein 1 (tulp1) gene

Cited by 18 publications

References 25 publications

Genome-Wide Identification and Expression Analysis of the Tubby-Like Protein Family in the Malus domestica Genome

Genome-Wide Identification and Expression Analysis of the Tubby-Like Protein Family in the Malus domestica Genome

Identification of TUB as a Novel Candidate Gene Influencing Body Weight in Humans

Insulin Phosphorylates Tyrosine Residue 464 of Tub and Translocates Tubby into the Nucleus in HIRcB Cells

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