NgUNC-119, Naegleria homologue of UNC-119, localizes to the flagellar rootlet

Chung, Sunglan; Kang, Sang Hun; Paik, Soon-Young; Lee, Joo Hun

doi:10.1016/j.gene.2006.09.032

Cited by 12 publications

(12 citation statements)

References 34 publications

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“…We also identified a trypanosome ortholog of UNC119 in the TbCEUN (Tb927.2.4580), and designated it as TbUNC119. TbUNC119 is a pathobiologically interesting molecule, because it has been reported that UNC119 has various functions and is conserved among various species including metazoans [13], [15], [16], [17]. Thus, in the present study, TbUNC119 was selected for further analysis in relation to parasite motility.…”

Section: Resultsmentioning

confidence: 99%

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TbUNC119 and Its Binding Protein Complex Are Essential for Propagation, Motility, and Morphogenesis of Trypanosoma brucei Procyclic Form Cells

et al. 2010

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Flagellum-mediated motility of Trypanosoma brucei is considered to be essential for the parasite to complete stage development in the tsetse fly vector, while the mechanism by which flagellum-mediated motility is controlled are not fully understood. We thus compared T. brucei whole gene products (amino acid sequence) with Caenorhabditis elegans UNC (uncoordinated) proteins, in order to find uncharacterized motility-related T. brucei genes. Through in silico analysis, we found 88 gene products which were highly similar to C. elegans UNC proteins and categorized them as TbCEUN (T. brucei gene products which have high similarity to C. elegans UNC proteins). Approximately two thirds of the 88 TbCEUN gene products were kinesin-related molecules. A gene product highly similar to C. elegans UNC119 protein was designated as TbUNC119. RNAi-mediated depletion of TbUNC119 showed no apparent phenotype. However, knock-down analysis of both TbUNC119 and its binding protein (TbUNC119BP) which was found by yeast two-hybrid analysis showed characteristic phenotypes, including reduced motility, morphological change (extended cell shape), and cellular apoptosis. Based on the observed phenotypes, possible function of the TbUNC119 and TbUNC119BP is discussed.

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Section: Resultsmentioning

confidence: 99%

“…A number of metazoan species and other organisms, including kinetoplastida, Naegleria and Chlamydomonas , share the UNC119 molecule [13], [15], [16], [17]. HsUNC119 is a signaling molecule that associates with interleukin (IL)-5 receptor α and Src family tyrosine kinases, and is essential for T cell activation [13], [26].…”

Section: Discussionmentioning

confidence: 99%

TbUNC119 and Its Binding Protein Complex Are Essential for Propagation, Motility, and Morphogenesis of Trypanosoma brucei Procyclic Form Cells

et al. 2010

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“…UNC119 homologs have been identified in plants (POC7 in C. reinhardtii, ( Keller et al, 2009)) and all animals, including unicellular protozoa such as Paramecium and Tetrahymena . Subcellularly, UNC119 homologs were identified in the basal body proteome of C. reinhardtii ( Keller et al, 2009), the flagellar rootlet of Naegleria (Chung et al, 2007), neurons of C. elegans (Maduro and Pilgrim, 1995) and in the mouse photoreceptor sensory cilium complex (Liu et al, 2007). …”

Section: Unc119 Supergene Familymentioning

confidence: 99%

Uncoordinated (UNC)119: Coordinating the trafficking of myristoylated proteins

et al. 2012

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The mechanism by which myristoylated proteins are targeted to specific subcellular membrane compartments is poorly understood. Two novel acyl-binding proteins, UNC119A and UNC119B, have been shown recently to function as chaperones/co-factors in the transport of myristoylated G protein α-subunits and src-type tyrosine kinases. UNC119 polypeptides feature an immunoglobulin-like β-sandwich fold that forms a hydrophobic pocket capable of binding lauroyl (C12) and myristoyl (C14) side chains. UNC119A in rod photoreceptors facilitates the transfer of transducin α subunits (Tα) from inner segment to outer segment membranes by forming an intermediate diffusible UNC119-Tα complex. Similar complexes are formed in other sensory neurons, as the G proteins ODR-3 and GPA-13 in C. elegans unc-119 mutants traffic inappropriately. UNC119B knockdown in IMCD3 cells prevents trafficking of myristoylated nephrocystin-3 (NPHP3), a protein associated with nephronophthisis, to cilia. Further, UNC119A was shown to transpot myristoylated src-type tyrosine kinases to cell membranes and to affect T-cell receptor (TCR) and interleukin-5 receptor (IL-5R) activities. These interactions establish UNC119 polypeptides as novel lipid-binding chaperones with specificity for a diverse subset of myristoylated proteins.

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“…UNC119 is 27 kDa polypeptide identified in the basal body proteome of C. reinhardtii 6 , the flagellar rootlet of Naegleria 7 , neurons of C. elegans 8 and the mouse photoreceptor sensory cilium complex 9 . unc-119 was first discovered in C. elegans on the basis of a spontaneous mutation affecting locomotion, feeding behavior and chemosensation 8 .…”

Section: Introductionmentioning

confidence: 99%

UNC119 is required for G protein trafficking in sensory neurons

et al. 2011

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SUMMARY UNC119 is widely expressed among vertebrates and invertebrates. Here we report that UNC119 recognized the acylated N-terminus of the rod photoreceptor transducin α-subunit (Tα) as well as C. elegans G proteins Odr-3 and Gpa-13. The crystal structure of human UNC119 at 1.95 Å resolution revealed an immunoglobulin-like β-sandwich fold. Pulldowns and isothermal titration calorimetry revealed a tight interaction between UNC119 and acylated Gα peptides. Co-crystallization of UNC119 with an acylated Tα N-terminal peptide at 2.0 Å revealed that the lipid chain is buried deeply into UNC119's hydrophobic cavity. UNC119 bound TαGTP inhibiting its GTPase activity, thereby providing a stable UNC119-TαGTP complex that is capable of diffusing from the inner segment back to the outer segment following light-induced translocation. UNC119 deletion in both mouse and C. elegans lead to G protein mislocalization. These results establish UNC119 as a novel Gα-subunit cofactor that is essential for G-protein trafficking in sensory cilia.

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NgUNC-119, Naegleria homologue of UNC-119, localizes to the flagellar rootlet

Cited by 12 publications

References 34 publications

TbUNC119 and Its Binding Protein Complex Are Essential for Propagation, Motility, and Morphogenesis of Trypanosoma brucei Procyclic Form Cells

TbUNC119 and Its Binding Protein Complex Are Essential for Propagation, Motility, and Morphogenesis of Trypanosoma brucei Procyclic Form Cells

Uncoordinated (UNC)119: Coordinating the trafficking of myristoylated proteins

UNC119 is required for G protein trafficking in sensory neurons

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