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In many species, taste receptors have shown loss of functions. The evolutionary process of which taste receptors lost their function is believed to be adaptive evolution where it is associated with feeding ecology to drive specialization and bifurcation of taste receptors. <ref name=":0">{{Cite journal|last=Feng|first=Ping|last2=Zhao|first2=HuaBin|date=2013-6|title=Complex evolutionary history of the vertebrate sweet/umami taste receptor genes|url=http://link.springer.com/10.1007/s11434-013-5811-5|journal=Chinese Science Bulletin|language=en|volume=58|issue=18|pages=2198–2204|doi=10.1007/s11434-013-5811-5|issn=1001-6538}}</ref> Out of all the taste receptors, bitter, sweet, and umami are shown to have a correlation between inactivation of taste receptors and feeding behavior. <ref name=":0" /> However, there are no strong evidences that support any vertebrates are missing the bitter taste receptor genes. <ref name=":0" />
= MicroProtein =
MicroProteins (miPs) are a class of protein with a single protein domain that are related to multidomain proteins. <ref name=":0">{{Cite journal|last=Bhati|first=Kaushal Kumar|last2=Blaakmeer|first2=Anko|last3=Paredes|first3=Esther Botterweg|last4=Dolde|first4=Ulla|last5=Eguen|first5=Tenai|last6=Hong|first6=Shin-Young|last7=Rodrigues|first7=Vandasue|last8=Straub|first8=Daniel|last9=Sun|first9=Bin|date=2018-04-18|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology|url=http://dx.doi.org/10.1007/s00018-018-2818-8|journal=Cellular and Molecular Life Sciences|volume=75|issue=14|pages=2529–2536|doi=10.1007/s00018-018-2818-8|issn=1420-682X}}</ref> MicroProteins regulate larger multidomain proteins at the post-translational level. <ref name=":1">{{Cite journal|last=Staudt|first=Annica-Carolin|last2=Wenkel|first2=Stephan|date=2010-12-10|title=Regulation of protein function by ‘microProteins’|url=http://dx.doi.org/10.1038/embor.2010.196|journal=EMBO reports|volume=12|issue=1|pages=35–42|doi=10.1038/embor.2010.196|issn=1469-221X}}</ref> MicroProteins are analogous to microRNAs  (miRNAs) and heterodimerize with their targets causing dominant and negative effects (Eguen). <ref name=":2">{{Cite journal|last=Eguen|first=T|last2=Straub|first2=D|last3=Graeff|first3=M|last4=Wenkel|first4=S|date=August 2015|title=MicroProteins: small size-big impact|url=|journal=Trends in Plant Science|volume=20|issue=8|pages=|doi=10.1016/j.tplants.2015.05.011|via=}}</ref> In animals and plants, microProteins have been found to greatly influence the biological processes. <ref name=":0" /> Because of microProteins dominant effects on their targets, microProteins are currently being studied for potential applications in biotechnology. <ref name=":0" />


== History ==
The first microProtein (miP) discovered was during a research in the early 1990s on genes for basic helix–loop–helix (bHLH) transcription factors from a murine erythroleukaemia cell cDNA library. <ref name=":1" /> The protein was found to be an inhibitor of DNA binding (Id), and it negatively regulate transcription factor complex. <ref name=":1" /> The Id protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain. <ref name=":0" /> The microProtein formed bHLH/HLH heterodimers which disrupted the functional basic helix–loop–helix (bHLH) homodimers. <ref name=":0" /> The first microProtein discovered in plants was the LITTLE ZIPPER (ZPR) protein. <ref name=":0" /> The LTTLE ZIPPPER protein contains a leucine zipper domain but does not have the domains required for DNA binding and transcription activation. <ref name=":0" /> Thus, LITTLE ZIPPER protein is analogous to the Id protein. <ref name=":0" /> Despite not all proteins being small, in 2011, this class of protein was given the named microProteins because their negative regulatory actions are similar to those of miRNAs. <ref name=":1" />


The sweet taste receptor is one of the taste receptors where the function has been lost. In mammals, the predominant sweet taste receptor is the Type 1 taste receptor Tas1r2/Tas1r3. <ref name=":1">{{Cite journal|last=Jiang|first=P.|last2=Josue|first2=J.|last3=Li|first3=X.|last4=Glaser|first4=D.|last5=Li|first5=W.|last6=Brand|first6=J. G.|last7=Margolskee|first7=R. F.|last8=Reed|first8=D. R.|last9=Beauchamp|first9=G. K.|date=2012-03-27|title=Major taste loss in carnivorous mammals|url=http://www.pnas.org/cgi/doi/10.1073/pnas.1118360109|journal=Proceedings of the National Academy of Sciences|language=en|volume=109|issue=13|pages=4956–4961|doi=10.1073/pnas.1118360109|issn=0027-8424|pmc=PMC3324019|pmid=22411809}}</ref> Some mammalian species such as cats and vampire bats have shown inability to taste sweet. <ref name=":1" /> In these species, the cause of loss of function of the sweet receptor is due to the pseudogenization of Tas1r2. <ref name=":1" /> The pseudogenization of Tas1r2 is also observed in non-mammalian species such as chickens and tongueless Western clawed frog, and these species also show the inability to taste sweet. <ref name=":1" /> The pseudogenization of Tas1r2 is widespread and independent in the order Carnivora. <ref name=":1" /> Many studies have shown that the pseduogenization of taste receptors is caused by a deleterious mutation in the open reading frames (ORF). <ref name=":2">{{Cite journal|last=Antinucci|first=Marco|last2=Risso|first2=Davide|date=2017-11-28|title=A Matter of Taste: Lineage-Specific Loss of Function of Taste Receptor Genes in Vertebrates|url=http://journal.frontiersin.org/article/10.3389/fmolb.2017.00081/full|journal=Frontiers in Molecular Biosciences|volume=4|doi=10.3389/fmolb.2017.00081|issn=2296-889X|pmc=PMC5712339|pmid=29234667}}</ref> In a study, it was found that in nonfeline carnivorous species, these species showed ORF-disrupting mutations of Tas1r2, and they occurred independently among the species. <ref name=":1" /> They also showed high variance in their lineages. <ref name=":1" /> It is hypothesized that the pseudogenization of Tas1r2 occurred through convergent evolution where carnivorous species lost their ability to taste sweet because of dietary behavior. <ref name=":1" /> Overall, the loss of function of the a taste receptor is a evolutionary process that occurred due to a dietary change in species. <ref name=":2" />
Evolutionary, the Id protein or proteins similar to Id are found in all animals. <ref name=":1" /> In plants, microProteins are only found in higher order. <ref name=":1" /> However, the homeodomain transcription factors that belong to the three-amino-acid loop-extension (TALE) family are targets of microProteins, and this homeodomain proteins are conserved in animals, plants, and fungi. <ref name=":1" />


== Structure ==
MicroProteins are generally small proteins with a single protein domain. <ref name=":0" /> <ref name=":2" /> However, not all microProteins are small, and the name was given because their actions are analogous to miRNAs. <ref name=":1" />


Umami is also a taste receptor where the function has been lost in many species. The predominant umami taste receptors are Tas1r1/Tas1r3. <ref name=":1" /> In two lineages of aquatic mammals including dolphins and sea lions, Tas1r1 has been found to be pseudogenized. <ref name=":1" /> The pseudogenization of Tas1r1 has also been found in terrestrial, carnivorous species. <ref name=":1" /> While the panda belongs to the order Carnivora, it is herbivorous where 99% of its diet is bamboo, and it cannot taste umami. <ref name=":3" /> Genome sequence of the panda shows that its Tas1r1 gene is pseudogenized. <ref name=":3">{{Cite journal|last=Zhao|first=H.|last2=Yang|first2=J.-R.|last3=Xu|first3=H.|last4=Zhang|first4=J.|date=2010-12-01|title=Pseudogenization of the Umami Taste Receptor Gene Tas1r1 in the Giant Panda Coincided with its Dietary Switch to Bamboo|url=https://academic.oup.com/mbe/article-lookup/doi/10.1093/molbev/msq153|journal=Molecular Biology and Evolution|language=en|volume=27|issue=12|pages=2669–2673|doi=10.1093/molbev/msq153|issn=0737-4038|pmc=PMC3108379|pmid=20573776}}</ref> In a study, it was found that in all species in the order Carnivora except the panda, the open reading frame was maintained. In panda, the nonsynonymous to synonymous substitutions ratio was found to be much higher than other species in order Carnivora. <ref name=":1" /> This data correlates with fossil records date of the panda to show where panda switched from carnivore to herbivore diet. <ref name=":1" /> Therefore, the loss of function of umami in panda is hypothesized to be caused by dietary change where the panda became less dependence on meat. <ref name=":1" /> However, these studies do not explain herbivores such as horses and cows that have retained the Tas1r1 receptor. <ref name=":3" />
== Function ==
The function of microProteins is post-translational regulators. <ref name=":1" /> MicroProteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes. <ref name=":2" /> Furthermore, microProteins can interact with any protein that require functional dimers to function normally. <ref name=":1" /> The primary targets of microProteins are transcription factors that bind to DNA as dimers. <ref name=":1" /> MicroProteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function. <ref name=":1" /> There are two types of miP inhibitions: homotypic miP inhibition and heterotypic miP inhibition. <ref name=":2" /> In homotypic miP inhibition, microProteins interact with proteins with similar protein-protein interaction (PPI) domain. <ref name=":2" /> In heterotypic miP inhibition, microProteins interact with proteins with different but compatible PPI domain. <ref name=":2" /> In both types of inhibition, microProteins interfere and prevent the PPI domains from interacting with their normal proteins. <ref name=":2" />

Revision as of 01:33, 25 April 2019

MicroProtein

MicroProteins (miPs) are a class of protein with a single protein domain that are related to multidomain proteins. [1] MicroProteins regulate larger multidomain proteins at the post-translational level. [2] MicroProteins are analogous to microRNAs  (miRNAs) and heterodimerize with their targets causing dominant and negative effects (Eguen). [3] In animals and plants, microProteins have been found to greatly influence the biological processes. [1] Because of microProteins dominant effects on their targets, microProteins are currently being studied for potential applications in biotechnology. [1]

History

The first microProtein (miP) discovered was during a research in the early 1990s on genes for basic helix–loop–helix (bHLH) transcription factors from a murine erythroleukaemia cell cDNA library. [2] The protein was found to be an inhibitor of DNA binding (Id), and it negatively regulate transcription factor complex. [2] The Id protein was 16 kDa and consisted of a helix-loop-helix (HLH) domain. [1] The microProtein formed bHLH/HLH heterodimers which disrupted the functional basic helix–loop–helix (bHLH) homodimers. [1] The first microProtein discovered in plants was the LITTLE ZIPPER (ZPR) protein. [1] The LTTLE ZIPPPER protein contains a leucine zipper domain but does not have the domains required for DNA binding and transcription activation. [1] Thus, LITTLE ZIPPER protein is analogous to the Id protein. [1] Despite not all proteins being small, in 2011, this class of protein was given the named microProteins because their negative regulatory actions are similar to those of miRNAs. [2]

Evolutionary, the Id protein or proteins similar to Id are found in all animals. [2] In plants, microProteins are only found in higher order. [2] However, the homeodomain transcription factors that belong to the three-amino-acid loop-extension (TALE) family are targets of microProteins, and this homeodomain proteins are conserved in animals, plants, and fungi. [2]

Structure

MicroProteins are generally small proteins with a single protein domain. [1] [3] However, not all microProteins are small, and the name was given because their actions are analogous to miRNAs. [2]

Function

The function of microProteins is post-translational regulators. [2] MicroProteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes. [3] Furthermore, microProteins can interact with any protein that require functional dimers to function normally. [2] The primary targets of microProteins are transcription factors that bind to DNA as dimers. [2] MicroProteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function. [2] There are two types of miP inhibitions: homotypic miP inhibition and heterotypic miP inhibition. [3] In homotypic miP inhibition, microProteins interact with proteins with similar protein-protein interaction (PPI) domain. [3] In heterotypic miP inhibition, microProteins interact with proteins with different but compatible PPI domain. [3] In both types of inhibition, microProteins interfere and prevent the PPI domains from interacting with their normal proteins. [3]

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Bhati, Kaushal Kumar; Blaakmeer, Anko; Paredes, Esther Botterweg; Dolde, Ulla; Eguen, Tenai; Hong, Shin-Young; Rodrigues, Vandasue; Straub, Daniel; et al. (2018-04-18). "Approaches to identify and characterize microProteins and their potential uses in biotechnology". Cellular and Molecular Life Sciences 75 (14): 2529–2536. doi:10.1007/s00018-018-2818-8. ISSN 1420-682X. http://dx.doi.org/10.1007/s00018-018-2818-8. 
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 Staudt, Annica-Carolin; Wenkel, Stephan (2010-12-10). "Regulation of protein function by ‘microProteins’". EMBO reports 12 (1): 35–42. doi:10.1038/embor.2010.196. ISSN 1469-221X. http://dx.doi.org/10.1038/embor.2010.196. 
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 Eguen, T; Straub, D; Graeff, M; Wenkel, S (August 2015). "MicroProteins: small size-big impact". Trends in Plant Science 20 (8). doi:10.1016/j.tplants.2015.05.011. 
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