LIG_Dynein_DLC8_1
ELM server details
ELM
blue dot
Functional site class:
Dynein (Light Chain) binding motif
Functional site description:
Conserved motif found in the intermediate chain of cytoplasmic Dynein complex (DIC) and many other proteins. Binds to DLC-8 (highly conserved 8-kDa light chain of Dynein).
ELM(s): LIG_Dynein_DLC8_1
LIG_Dynein_DLC8_1 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) 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: [KR].TQT
Present in taxon(s): Homo sapiens  Drosophila pseudoobscura  Schizosaccharomyces pombe  Eukaryota  Mus musculus  Plasmodium falciparum  Takifugu rubripes  Arabidopsis thaliana  Drosophila melanogaster  Saccharomyces cerevisiae  
Not represented in taxon(s):

o See 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 partners exist and that DLC-8 binding proteins contain the consensus sequence (K/R)XTQT. The motif interacts with the common target-accepting grooves of DCL-8 dimer.The motif forms a beta-strand structure in the DLC-8-target peptide complex. Because it binds to a large number of functionally unrelated proteins DCL-8 is believed to act as a multifunctional regulatory protein.

o Selected references

Fan J, Zhang Q, Tochio H, Li M, Zhang M
Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain.
J Mol Biol 2001 Feb 9;306(1) : 97-108.
PMID: 11178896

Lo KW, Naisbitt S, Fan JS, Sheng M, Zhang M
The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif.
J Biol Chem 2001 Apr 27;276(17) : 14059-66.
PMID: 11148209

o This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process
  microtubule-based movement
Cellular Component
  cytosol
  cytoplasmic dynein complex
  dynein complex
Molecular Function
  protein binding
  dynein light chain binding

 

o Instances for LIG_Dynein_DLC8_1

SequencePositionSubsequence
(Click for evidence information)
PDBGene NameProtein DescriptionOrganism
ZMY11_HUMAN 413-417 PRMLHRSTQTTNDGVC - Name=ZMYND11; Synonyms=BS69; Zinc finger MYND domain-containing protein 11 (Adenovirus 5 E1A- binding protein) (BS69 protein). Homo sapiens (Human).
BIM_HUMAN 112-116 PMSCDKSTQTPSPPCQ - Name=BCL2L11; Synonyms=BIM; Bcl-2-like protein 11 (Bcl2-interacting mediator of cell death). Homo sapiens (Human).
SWA_DROPS 276-280 PASVPKATQTDHELLS - Name=swa; ORFNames=GA17446; Protein swallow. Drosophila pseudoobscura (Fruit fly).
DC1I1_MOUSE 151-155 VVSYSKETQTPLATHQ - Name=Dync1i1; Synonyms=Dnci1, Dncic1; Cytoplasmic dynein 1 intermediate chain 1 (Dynein intermediate chain 1, cytosolic) (DH IC-1) (Cytoplasmic dynein intermediate chain 1). Mus musculus (Mouse).