Disease relevance of DYNLL1

• Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein [1].

High impact information on DYNLL1

• We screened an expression library for proteins that bind the PTH mRNA 3'-UTR, and the sequence of 1 clone was identical to that of the dynein light chain LC8, a component of the dynein complexes that translocate cytoplasmic components along microtubules [2].

Chemical compound and disease context of DYNLL1

• We demonstrate the strong binding of two herpesvirus polypeptides, the human adenovirus protease, vaccinia virus polymerase, human papillomavirus E4 protein, yam mosaic virus polyprotein, human respiratory syncytial virus attachment glycoprotein, human coxsackievirus capsid protein and the product of the AMV179 gene of an insect poxvirus to LC8 [3].

Biological context of DYNLL1

• The LC8-binding domain was mapped to a short peptide segment immediately N-terminal to the kinetochore localization region of 53BP1 [4].
• We have performed a fine mapping of the 8 kDa dynein light chain (LC8) binding sites throughout the development of a library of consecutive synthetic dodecapeptides covering the amino acid sequences of the various proteins known to interact with this dynein member according to the yeast two hybrid system [5].
• The structure provides key insights into dimerization of and peptide binding by the multifunctional PIN/LC8 protein [6].
• The N-terminal domain of the intermediate chain, IC1-289, contains the binding sites for the light chains, and is a highly disordered monomer but gains helical structure upon binding to light chains LC8 and Tctex-1 [7].

Anatomical context of DYNLL1

• Interestingly, we found that LC8a co-localizes with TRPS1 in dot-like structures in the cell nucleus [8].
• The cytoskeletal organization and dynamics of this syncytium are poorly understood, but predominant motor components are the LC8 class of cytoplasmic dynein light chains (DLC) [9].

Associations of DYNLL1 with chemical compounds

• Yeast two-hybrid analysis has revealed that in brain, LC8 associates directly with several proteins such as neuronal nitric oxide synthase, guanylate kinase domain-associated protein and gephyrin [10].

Physical interactions of DYNLL1

• The LC8-binding domain is completely separated from the p53-binding domain in 53BP1 [4].

Other interactions of DYNLL1

• Unlike other known LC8-binding proteins, 53BP1 contains two distinct LC8-binding motifs that are arranged in tandem [4].
• The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation [4].
• S. pombe contains a homolog of the 8-kDa dynein light chain, Dlc2 [11].
• The structure of the protein known both as neuronal nitric oxide synthase inhibitory protein, PIN (protein inhibitor of nNOS), and also as the 8 kDa dynein light chain (LC8) has been solved by X-ray diffraction [6].
• We found that two distinct regions of TRPS1 can physically interact with the dynein light chain 8 protein, LC8a, that are at least 458 amino acids apart from each other [8].

Analytical, diagnostic and therapeutic context of DYNLL1

• Recombinant LC8 binds PTH mRNA 3'-UTR, as shown by RNA electrophoretic mobility shift assay [2].
• Northern blot analysis and epitope tagging show that the hdlc1 (for human dynein light chain 1, or Dynll1/2) gene is ubiquitously expressed and that the human dynein light chain 1 is localized in the cytoplasm. hdlc1 (for human dynein light chain 1, or Dynll1/2) maps to 14q24 [12].

References