scholarly journals HA-tagging of putative flagellar proteins inChlamydomonas reinhardtiiidentifies a novel protein of intraflagellar transport complex B

2009 ◽  
Vol 66 (8) ◽  
pp. 469-482 ◽  
Author(s):  
Karl-Ferdinand Lechtreck ◽  
Scott Luro ◽  
Junya Awata ◽  
George B. Witman
Keyword(s):  
Intraflagellar Transport ◽  
Flagellar Proteins ◽  
Transport Complex ◽  
Novel Protein

scholarly journals Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly

2019 ◽  
Vol 38 (9) ◽  
Author(s):  
Stefanie Wachter ◽  
Jamin Jung ◽  
Shahaan Shafiq ◽  
Jerome Basquin ◽  
Cécile Fort ◽  
...  
Keyword(s):  
Intraflagellar Transport ◽  
Transport Complex

scholarly journals Interaction of mouse TTC30/DYF-1 with multiple intraflagellar transport complex B proteins and KIF17

2013 ◽  
Vol 319 (14) ◽  
pp. 2275-2281 ◽  
Author(s):  
Paul W. Howard ◽  
Shall F. Jue ◽  
Richard A. Maurer
Keyword(s):  
Intraflagellar Transport ◽  
Transport Complex

scholarly journals Interactions between TULP3 tubby domain cargo site and ARL13B amphipathic helix promote lipidated protein transport to cilia

2021 ◽  
Author(s):  
Vivek Reddy Palicharla ◽  
Sun-hee Hwang ◽  
Bandarigoda N. Somatilaka ◽  
Hemant B. Badgandi ◽  
Emilie Legue ◽  
...  
Keyword(s):  
Protein Transport ◽  
Transmembrane Proteins ◽  
Intraflagellar Transport ◽  
Amphipathic Helix ◽  
Cargo Transport ◽  
Family Protein ◽  
Associated Proteins ◽  
Sorting Motif ◽  
Necessary And Sufficient ◽  
Transport Complex

The tubby family protein-TULP3 coordinates with the intraflagellar transport complex-A (IFT-A) in trafficking certain transmembrane proteins to cilia. These transmembrane cargoes have short motifs that are necessary and sufficient for TULP3-mediated trafficking. However, whether TULP3 regulates trafficking of membrane-associated proteins is not well understood. Here we show that TULP3 is required for transport of the atypical GTPase ARL13B into cilia, and for ciliary enrichment of ARL13B-dependent farnesylated and myristoylated proteins. ARL13B transport requires TULP3 binding to IFT-A core but not to phosphoinositides, unlike transmembrane cargo transport that requires binding to both by TULP3. A conserved lysine in TULP3's tubby domain mediates direct ARL13B binding and trafficking of lipidated and transmembrane cargoes. An N-terminal amphipathic helix in ARL13B flanking the palmitoylation site mediates binding to TULP3 and directs trafficking to cilia even in absence of palmitoylation and RVxP sorting motif. Therefore, TULP3 transports transmembrane proteins and ARL13B into cilia by capture of short sequences through a shared tubby domain site.

scholarly journals IFT20 Links Kinesin II with a Mammalian Intraflagellar Transport Complex That Is Conserved in Motile Flagella and Sensory Cilia

2003 ◽  
Vol 278 (36) ◽  
pp. 34211-34218 ◽  
Author(s):  
Sheila A. Baker ◽  
Katie Freeman ◽  
Katherine Luby-Phelps ◽  
Gregory J. Pazour ◽  
Joseph C. Besharse
Keyword(s):  
Intraflagellar Transport ◽  
Sensory Cilia ◽  
Transport Complex

scholarly journals Characterization of the Intraflagellar Transport Complex B Core

2005 ◽  
Vol 280 (30) ◽  
pp. 27688-27696 ◽  
Author(s):  
Ben F. Lucker ◽  
Robert H. Behal ◽  
Hongmin Qin ◽  
Laura C. Siron ◽  
W. David Taggart ◽  
...  
Keyword(s):  
Intraflagellar Transport ◽  
Transport Complex

scholarly journals Defective flagellar assembly and length regulation in LF3 null mutants in Chlamydomonas

2003 ◽  
Vol 163 (3) ◽  
pp. 597-607 ◽  
Author(s):  
Lai-Wa Tam ◽  
William L. Dentler ◽  
Paul A. Lefebvre
Keyword(s):  
Immunofluorescence Microscopy ◽  
Intraflagellar Transport ◽  
Wild Type ◽  
Western Blots ◽  
Functional Complex ◽  
Length Regulation ◽  
Flagellar Assembly ◽  
Unequal Length ◽  
Null Mutants ◽  
Novel Protein

Four long-flagella (LF) genes are important for flagellar length control in Chlamydomonas reinhardtii. Here, we characterize two new null lf3 mutants whose phenotypes are different from previously identified lf3 mutants. These null mutants have unequal-length flagella that assemble more slowly than wild-type flagella, though their flagella can also reach abnormally long lengths. Prominent bulges are found at the distal ends of short, long, and regenerating flagella of these mutants. Analysis of the flagella by electron and immunofluorescence microscopy and by Western blots revealed that the bulges contain intraflagellar transport complexes, a defect reported previously (for review see Cole, D.G., 2003. Traffic. 4:435–442) in a subset of mutants defective in intraflagellar transport. We have cloned the wild-type LF3 gene and characterized a hypomorphic mutant allele of LF3. LF3p is a novel protein located predominantly in the cell body. It cosediments with the product of the LF1 gene in sucrose density gradients, indicating that these proteins may form a functional complex to regulate flagellar length and assembly.

scholarly journals Crystal structure of the intraflagellar transport complex 25/27

2011 ◽  
Vol 30 (10) ◽  
pp. 1907-1918 ◽  
Author(s):  
Sagar Bhogaraju ◽  
Michael Taschner ◽  
Michaela Morawetz ◽  
Claire Basquin ◽  
Esben Lorentzen
Keyword(s):  
Crystal Structure ◽  
Intraflagellar Transport ◽  
Transport Complex

scholarly journals The ubiquitin conjugation system is involved in the disassembly of cilia and flagella

2009 ◽  
Vol 186 (4) ◽  
pp. 601-613 ◽  
Author(s):  
Kaiyao Huang ◽  
Dennis R. Diener ◽  
Joel L. Rosenbaum
Keyword(s):  
Intraflagellar Transport ◽  
Active Role ◽  
Cyclic Guanosine Monophosphate ◽  
Guanosine Monophosphate ◽  
Signaling Proteins ◽  
Conjugation System ◽  
Ubiquitin Conjugating Enzyme ◽  
Ubiquitin Conjugation ◽  
Flagellar Proteins ◽  
Cilia And Flagella

The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flagellar proteins is an integral part of flagellar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flagellar proteins increase during flagellar resorption, especially in intraflagellar transport (IFT) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by IFT. Substrates of the ubiquitin conjugation system include α-tubulin (but not β-tubulin), a dynein subunit (IC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate–dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flagellar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella.

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