The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Functional site class:
Dynein (Light Chain) binding motifs
Functional site description:
Motifs are found in the intermediate chain of cytoplasmic Dynein complex (DIC) and many other proteins that bind to light chains. The best characterised motif is the KxTQT motif that binds to DLC-8 (highly conserved 8-kDa light chain of Dynein).
ELM Description:
[KR]xTQT is a conserved motif found in the intermediate chain of Dynein complex (DIC) and many other proteins. It participates in the precise assembly essential to dynein motor proper functioning. It binds to DLC-8 (highly conserved 8-kDa light chain of Dynein) by beta-augmentation as an extended beta-strand. The motif is also found in viral proteins, suggesting that DLC-8 might be involved in dynein mediated retrograde transport of these proteins along the microtubules in infected cells.
Pattern: [^P].[KR].TQT
Pattern Probability: 0.0000226
Present in taxons: Arabidopsis thaliana Drosophila melanogaster Drosophila pseudoobscura Eukaryota Homo sapiens Mus musculus Plasmodium falciparum Saccharomyces cerevisiae Schizosaccharomyces pombe Takifugu rubripes
Interaction Domain:
Dynein_light (PF01221) Dynein light chain type 1 (Stochiometry: 1 : 1)
PDB Structure: 2P2T
o See 9 Instances for LIG_Dynein_DLC8_1
o Abstract
Dynein is a large, multisubunit molecular motor that translocates cargoes toward the minus end of microtubules. It contains 2 heavy chains (DHC), several intermediate chains (DIC) and light intermediate chains (DLIC) and a number of light chains (DLC). Specific assembly of the various subunits has to be precise to ensure functioning of Dynein. The intermediate chain (DIC) of cytoplasmic dynein binds to the highly conserved 8-kDa light chain (DLC-8) through a highly conserved 10 aa stretch (reads SYSKETQTPL). A yeast 2-hybrid screen using DLC-8 as bait showed that a wide variety of additional partner candidates exist and that DLC-8 binding proteins contain the consensus sequence (K/R)XTQT. The motif interacts with the common target-accepting grooves of the DLC-8 dimer. The motif binds by beta-augmentation to form a beta-stranded structure in the DLC-8-target peptide complex. The backbone hydrogen bonds are to one DLC-8 monomer while the Q sidechain makes polar interactions with the second molecule. Because it binds to a large number of functionally unrelated proteins, DCL-8 is believed to act as a multifunctional regulatory protein.
A variant motif in nNOS - GIQVD - is found to bind in a similar manner to DLC-8. In yeast, a repeating (VLT)QT motif in the nuclear pore protein nup159 binds to the DLC Dyn2. A KxTQV motif in DIC binds to the DLC TcTex1. It therefore seems likely that other variants of the Q-based DLC interaction motifs will be found.
o 6 selected references:

o 6 GO-Terms:

o 9 Instances for LIG_Dynein_DLC8_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
Q15326 ZMYND11
451 457 ASSPRMLHRSTQTTNDGVCQ TP 5 Homo sapiens (Human)
O43521 BCL2L11
110 116 SPAPMSCDKSTQTPSPPCQA TP 4 Homo sapiens (Human)
O43521-2 BCL2L11
50 56 SPAPMSCDKSTQTPSPPCQA TP 5 Homo sapiens (Human)
P22363 P
142 148 PPRRSSEDKSTQTTGRELKK TP 1 Rabies virus CVS-11
O88485 Dync1i1
149 155 PREVVSYSKETQTPLATHQS TP 6 Mus musculus (House mouse)
Q13409 DYNC1I2
156 162 PREIVTYTKETQTPVMAQPK TP 1 Homo sapiens (Human)
Q24246 sw
128 134 PKETLVYTKQTQTTSTGGGN TP 2 Drosophila melanogaster (Fruit fly)
P40688 swa
289 295 HIRSATSAKATQTDFLVDTI TP 8 Drosophila melanogaster (Fruit fly)
Q9U9I5 swa
281 287 FCPPASVPKATQTDHELLSH TP 0 Drosophila pseudoobscura pseudoobscura
Please cite: The eukaryotic linear motif resource - 2018 update. (PMID:29136216)

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