Dynein light chain 2, cytoplasmic (DYNLL2)
The protein contains 89 amino acids for an estimated molecular weight of 10350 Da.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
Aggrephagy
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Apoptotic process
Cilium assembly
Endoplasmic reticulum to Golgi vesicle-mediated transport
Intraciliary transport involved in cilium assembly
Intrinsic apoptotic signaling pathway
Macroautophagy
Microtubule-based process
Mitotic spindle organization
Organelle organization
Positive regulation of ATP-dependent microtubule motor activity, plus-end-directed
Positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
Sister chromatid cohesion
Synaptic target recognition
Transport
Transport along microtubule
Viral life cycle
The reference OMIM entry for this protein is 608942
Dynein, light chain, lc8 type, 2; dynll2
Dynein light chain 2; dlc2
CLONING
Using yeast 2-hybrid analysis with the postsynaptic scaffold protein gephyrin (GPH; 603930) as bait, Fuhrmann et al. (2002) identified rat dynein light chain-2 (Dlc2). Dlc2 encodes an 89-amino acid protein that shows 93% and 100% identity to rat Dlc1 (DNCL1; 601562) and human DLC2, respectively. Coimmunoprecipitation and GST pull-down assays confirmed that Dlc2 binds with Gph, and yeast 2-hybrid analysis showed that Dlc2 binds to residues 181-243 of Gph, in the central linker domain.GENE FUNCTION
Using immunofluorescence, Fuhrmann et al. (2002) showed that both recombinant and endogenous Dlc2 colocalize with Gph in HEK293 cells. In primary hippocampal neurons, Dlc2 localized to the cytoplasm in a granular staining pattern and to the plasma membrane of dendrites and cell bodies in a punctate staining pattern. The pattern of Dlc2 membrane staining overlapped that of synaptophysin (313475) and partially overlapped that of Gph. Electron microscopy of spinal cord neurons showed that Dlc2 localizes to the edges of postsynaptic differentiations, along cytoskeletal structures, and at the edge of the Golgi apparatus. Wildtype Gph and Gph lacking the Dlc-binding domain expressed in hippocampal neurons showed similar staining patterns, suggesting that Dlc2 binding is not required for Gph localization.MAPPING
By genomic sequence analysis, Pazour et al. (2006) mapped the DLC2 gene to chromosome 17q23.2. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 608942 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed