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 , 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 TLPs identified three types of conserved motifs. Motif 1 and 2, the signature motifs in the confirmed TLPs, were always present in TLPs, while motif 3 was absent from group B. Homology modeling indicated that the tubby domain of most TLPs had a closed β barrel, as in animal tubby domains. Expression profiling revealed that the TLP genes were expressed in multiple organs and were abundant in roots, stems, and leaves but low in flowers. An analysis of -acting elements showed that elements related to the stress response were prevalent in the promoter sequences of s. Expression profiling by qRT-PCR indicated that almost all s were up-regulated at some extent under abiotic stress, exogenous ABA and HO treatments in leaves and roots, though different TLP 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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http://dx.doi.org/10.3389/fpls.2016.01693 | DOI Listing |
Mol Biol Cell
January 2025
Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
The primary cilium is a paradigmatic subcellular compartment at the nexus of numerous cellular and morphogenetic pathways. The tubby family protein TULP3 acts as an adapter of the intraflagellar transport complex A in transporting integral membrane and membrane-associated lipidated proteins into cilia. However, the mechanisms by which TULP3 coordinates ciliary transport of diverse cargoes is not well understood.
View Article and Find Full Text PDFFunct Integr Genomics
September 2024
Provincial Key Laboratory of the Biodiversity Study and Ecology Conservation in Southwest Anhui, Anqing, 246133, China.
Tubby-like proteins (TLPs) are a group of proteins found in both eukaryotes and prokaryotes. They are significant in various physiological and biochemical processes, especially in plants' response to abiotic stress. However, the role of TLP in foxtail millet (Setaria italica) remains unclear.
View Article and Find Full Text PDFCell Rep
May 2024
Department of Psychiatry and Behavioral Sciences, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address:
Opioid receptors are therapeutically important G protein-coupled receptors (GPCRs) with diverse neuromodulatory effects. The functional consequences of opioid receptor activation are known to depend on receptor location in the plasma membrane, but mechanisms mediating selective localization of receptors to any particular membrane domain remain elusive. Here, we demonstrate the targeting of the mu opioid receptor (MOR) to the primary cilium, a discrete microdomain of the somatic plasma membrane, both in vivo and in cultured cells.
View Article and Find Full Text PDFPlants (Basel)
March 2024
Biological Sciences Department, Suny Old Westbury, Old Westbury, NY 11568, USA.
The Tubby-like proteins (TLPs) gene family is a group of transcription factors found in both animals and plants. In this study, we identified twelve TLPs, divided into six groups based on conserved domains and evolutionary relationships. We predicted cis-regulatory elements involved in light, hormone, and biotic and abiotic stresses.
View Article and Find Full Text PDFJ Biol Chem
January 2024
Faculty of Medicine, Institute for Medical Research Israel-Canada (IMRIC), Edmond and Lily Safra Center for Brain Sciences (ELSC), The Hebrew University, Jerusalem, Israel. Electronic address:
Sterols are hydrophobic molecules, known to cluster signaling membrane-proteins in lipid rafts, while methyl-β-cyclodextrin (MβCD) has been a major tool for modulating membrane-sterol content for studying its effect on membrane proteins, including the transient receptor potential (TRP) channels. The Drosophila light-sensitive TRP channels are activated downstream of a G-protein-coupled phospholipase Cβ (PLC) cascade. In phototransduction, PLC is an enzyme that hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) generating diacylglycerol, inositol-tris-phosphate, and protons, leading to TRP and TRP-like (TRPL) channel openings.
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