Functional diversification of the Tubby-like protein gene families (TULPs) during eukaryotic evolution

Lai, Chia-Ping; Chen, Po-Hsuan; Huang, Jen‐Pan; Tzeng, Yun-Huei; Chaw, Shu‐Miaw; Shaw, Jei‐Fu

doi:10.1016/j.bcab.2011.08.001

Cited by 11 publications

(8 citation statements)

References 38 publications

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“…The TLPs from different classes are very different in function (Lai et al 2012). The F-box family proteins are characterized by a signature of the F-box domain (Jia et al 2013).…”

Section: Discussionmentioning

confidence: 99%

“…The F-box proteins are involved in ubiquitin-dependent proteolysis in cell cycle regulation and signal transduction, which function in many aspects such as cell elongation and division, injury response, floral differentiation, circadian clock and response to the plant growth regulators auxin and jasmonic acid in plants (Craig and Tyers 1999; del Pozo and Estelle 2000; Ho et al 2008; Baute et al 2017). Relatively to the F-box proteins, most plant TLPs remain a mystery in function although they have been found across plant species (Lai et al 2012; Wang et al 2018). The limited reports indicate that plant TLPs play roles in responses to multifarious stresses including biotic and abiotic stress (Bhushan et al 2007; Kou et al 2009; Wardhan et al 2012; Bao et al 2014; Wang et al 2018; Xu et al 2019).…”

Section: Discussionmentioning

confidence: 99%

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Decrypting tubby-like protein gene family of multiple functions in starch root crop cassava

et al. 2019

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Tubby-like proteins (TLPs) are ubiquitous in eukaryotes and function in abiotic stress tolerance of some plants. Cassava (Manihot esculenta Crantz) is a high-yield starch root crop and has a high tolerance to poor soil conditions and abiotic stress. However, little is known about TLP gene characteristics and their expression in cassava. We identified cassava TLP genes, MeTLPs, and further analysed structure, duplication, chromosome localization and collinearity, cis-acting elements in the promoter regions and expression patterns of MeTLPs, and three-dimensional structure of the encoded proteins MeTLPs. In conclusion, there is a MeTLP family containing 13 members, which are grouped into A and C subfamilies. There are 11 pairs of MeTLPs that show the duplication which took place between 10.11 and 126.69 million years ago. Two MeTLPs 6 and 9 likely originate from one gene in an ancestral species, may be common ancestors for other MeTLPs and would most likely not be eligible for ubiquitin-related protein degradation because their corresponding proteins (MeTLPs 6 and 9) have no the F-box domain in the N-terminus. MeTLPs feature differences in the number from TLPs in wheat, apple, Arabidopsis, poplar and maize, and are highlighted by segmental duplication but more importantly by the chromosomal collinearity with potato StTLPs. MeTLPs are at least related to abiotic stress tolerance in cassava. However, the subtle differences in function among MeTLPs are predictable partly because of their differential expression profiles, which are coupled with various cis‑acting elements existing in the promoter regions depending on genes.

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“…The TLPs from different classes are very different in function (Lai et al 2012). The F-box family proteins are characterized by a signature of the F-box domain (Jia et al 2013).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Decrypting tubby-like protein gene family of multiple functions in starch root crop cassava

et al. 2019

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“…Tulp1 is a member of a family of related proteins named tubby-like proteins (Tulps) and encompasses the founding member Tub and the related Tulps, Tulp1 – 4. [38,39]. Mutations in human TULP1 have been associated with early-onset, severe retinitis pigmentosa (RP) and Leber congenital amaurosis (LCA) [40–44].…”

Section: Discussionmentioning

confidence: 99%

Photoreceptor Compartment-Specific TULP1 Interactomes

Ebke

Sinha

Pauer

et al. 2021

Preprint

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Photoreceptors are highly compartmentalized cells with large amounts of proteins synthesized in the inner segment (IS) and transported to the outer segment (OS) and synaptic terminal. Tulp1 is a photoreceptor-specific protein localized to the IS and synapse. In the absence of Tulp1, sev-eral OS-specific proteins are mislocalized and synaptic vesicle recycling is impaired. To better understand the involvement of Tulp1 in protein trafficking, our approach was to physically iso-late Tulp1-containing photoreceptor compartments by serial tangential sectioning of retinas and to identify compartment-specific Tulp1 binding partners by immunoprecipitation followed by liquid chromatography tandem mass spectrometry. Our results indicate that Tulp1 has two dis-tinct interactomes. We report the identification of: 1) an IS-specific interaction between Tulp1 and the motor protein Kinesin family member 3a (Kif3a), 2) a synaptic-specific interaction be-tween Tulp1 and the scaffold protein Ribeye, and 3) an interaction between Tulp1 and the cyto-skeletal protein Microtubule-associated protein 1B (MAP1B) in both compartments. Immuno-localization studies in the wild-type retina indicate that Tulp1 and its binding partners co-localize to their respective compartments. Our observations are compatible with Tulp1 functioning in protein trafficking in multiple photoreceptor compartments, likely as an adapter molecule linking vesicles to molecular motors and the cytoskeletal scaffold.

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“…In contrast to the conserved C-terminal tubby domain, motifs at N-terminus of TLPs (e.g., F-box, WD40 repeat, or SOCS box) differ greatly across species. According to previous studies, TLPs can be divided into three classes based on phylogenetic trees (Gagne et al, 2002;Lai et al, 2012). Although plants have more TLPs than do animals, the N-termini of animal TLPs are highly divergent while the majority of plant TLPs contain N-terminal F-box domains and are relatively conserved in this region (Gagne et al, 2002;Lai et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification of the Tubby-Like Protein (TLPs) family in medicinal model plant Salvia miltiorrhiza

Wang

Cheng

et al. 2021

PeerJ

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Tubby-Like Proteins (TLPs) are important transcription factors with many functions and are found in both animals and plants. In plants, TLPs are thought to be involved in the abiotic stress response. To reveal the potential function of TLPs in the medicinal model plant Salvia miltiorrhiza, we identified 12 S. miltiorrhiza TLPs (SmTLPs) and conducted a comprehensive analysis. We examined SmTLP gene structure, protein structure, phylogenetics, and expression analysis. Our results show that all SmTLPs, except SmTLP11, have a complete typical Tub domain. Promoter analysis revealed that most SmTLPs are involved in hormone and abiotic stress responses. Expression analysis revealed that the 12 SmTLPs could be divided into three categories: those specifically expressed in roots, those specifically expressed in stems, and those specifically expressed in leaves. Additional studies have shown that SmTLP10 may play an important role in the plant cold resistance, while SmTLP12 may be involved in the S. miltiorrhiza ABA metabolic pathway. Our study represents the first comprehensive investigation of TLPs in S. miltiorrhiza. These data may provide useful clues for future studies and may support the hypotheses regarding the role of TLPs in plant abiotic stress process. All in all, we may provide a reference for improving S. miltiorrhiza quality using genetic engineering technology.

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Functional diversification of the Tubby-like protein gene families (TULPs) during eukaryotic evolution

Cited by 11 publications

References 38 publications

Decrypting tubby-like protein gene family of multiple functions in starch root crop cassava

Decrypting tubby-like protein gene family of multiple functions in starch root crop cassava

Photoreceptor Compartment-Specific TULP1 Interactomes

Genome-wide identification of the Tubby-Like Protein (TLPs) family in medicinal model plant Salvia miltiorrhiza

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