Proteomic identification of brain proteins that interact with dynein light chain LC8

  title={Proteomic identification of brain proteins that interact with dynein light chain LC8},
  author={Inmaculada Navarro-L{\'e}rida and M{\'o}nica Mart{\'i}nez Moreno and Fernando Roncal and Francisco Gavilanes and Juan P. Albar and Ignacio Rodrı́guez-Crespo},
Cytoplasmic dynein is a large minus end‐directed microtubule motor that translocates cargos towards the minus end of microtubules. Light chain 8 of the dynein machinery (LC8) has been reported to interact with a large variety of proteins that possess K/RSTQT or GIQVD motifs in their sequence, hence permitting their transport in a retrograde manner. Yeast two‐hybrid analysis has revealed that in brain, LC8 associates directly with several proteins such as neuronal nitric oxide synthase… 

Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A

Using DYNLL1 as bait in a yeast two‐hybrid screen with a human heart library, GRINL1A (ionotropic glutamate receptor N‐methyl‐d‐aspartate‐like 1A), a homolog of the ionotropic glutamate receptors N‐ methyl d‐ aspartate, is identified as a DYNll1 binding partner and data suggest that additional DynLL1‐binding partners are present near this glutamate channel homolog.

DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond

The most prominent LC8 function is to promote dimerization of their binding partners that are often scaffold proteins of various complexes, including the intermediate chains of the dynein motor complex.

Structural and thermodynamic characterization of a cytoplasmic dynein light chain–intermediate chain complex

The structure and thermodynamic analysis of a complex of LC8 and TcTex1 associated with their intermediate chain scaffold suggest that, in the dynein complex, the LCs do not bind cargo, in apparent disagreement with a role for LCs in dyne in cargo binding interactions.

Dynein light chain family in Tetrahymena thermophila.

This study provides a complete description of the different genes and isoforms of the dynein light chains that are expressed in Tetrahymena, a model organism in which the targeted manipulation of genes is straightforward.

Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast

It is shown that cells of the yeast Yarrowia lipolytica deleted for the gene encoding the homologue of Dyn2p are impaired in peroxisome function and biogenesis, and evidence is provided that Dyn 2p acts in cooperation with the peroxISomal matrix protein import docking complex to effect optimal matrixprotein import.

Dynein Light Chain LC8 Regulates Syntaphilin-Mediated Mitochondrial Docking in Axons

This study provides new mechanistic insights into controlling mitochondrial mobility through a dynamic interaction between the mitochondrial docking receptor and axonal cytoskeleton through the role of dynein light chain LC8.

Serine 88 Phosphorylation of the 8-kDa Dynein Light Chain 1 Is a Molecular Switch for Its Dimerization Status and Functions*

It is discovered that phosphorylation of Ser88, which juxtapose each other at the interface of the DLC dimer, disrupts DLC1 dimer formation and consequently impairs its interaction with Bim, revealing a previously unrecognized regulatory mechanism of DLC1 in which the Ser88osphorylation acts as a molecular switch for the transition of DLC 1 from dimer to monomer.

Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex

Dyn2 is a previously undescribed nucleoporin that functions as molecular glue to dimerize and stabilize the Nup82–Nsp1–Nup159 complex, a module of the cytoplasmic pore filaments.

Systematic identification of recognition motifs for the hub protein LC8

The “LC8Pred” algorithm, a algorithm that identifies critical residues flanking the anchor and parses random sequences to predict LC8-binding motifs with ∼78% accuracy, is developed, significantly expand the scope of the LC8 hub interactome.