Microtubule-associated protein RP/EB family member 1 (MAPRE1)
The protein contains 268 amino acids for an estimated molecular weight of 29999 Da.
Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes (PubMed:12388762). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). May play a role in cell migration (By similarity). (updated: Jan. 31, 2018)
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.
(right-click above to access to more options from the contextual menu)
Biological Process
Cell division
Cell migration
Cell population proliferation
Ciliary basal body-plasma membrane docking
G2/M transition of mitotic cell cycle
Microtubule bundle formation
Microtubule polymerization
Mitotic cell cycle
Mitotic nuclear division
Mitotic spindle organization
Negative regulation of microtubule binding
Negative regulation of microtubule polymerization
Non-motile cilium assembly
Organelle organization
Positive regulation of cell migration
Positive regulation of microtubule plus-end binding
Positive regulation of microtubule polymerization
Protein localization
Protein localization to centrosome
Protein localization to microtubule
Protein localization to microtubule plus-end
Regulation of G2/M transition of mitotic cell cycle
Regulation of microtubule polymerization or depolymerization
Sister chromatid cohesion
Spindle assembly
The reference OMIM entry for this protein is 603108
Microtubule-associated protein, rp/eb family, member 1; mapre1
End-binding protein 1; eb1
Adenomatous polyposis coli-binding protein eb1
DESCRIPTION
MAPRE1 is a regulator of microtubule dynamics that localizes at both the growing plus ends of microtubules and the centrosome. It is involved in a variety of cellular processes, including establishment and maintenance of cell polarity, search and capture of chromosomes during mitosis, and positioning of the mitotic spindle during asymmetric cell division (Sun et al., 2008).CLONING
EB1 is a 30- to 35-kD protein that was isolated in a yeast 2-hybrid screen by its binding to the C-terminal domain of APC (611731) (Su et al., 1995), a domain that is deleted in the majority of familial and sporadic forms of colon carcinoma.GENE FAMILY
By genomic sequence analysis, Su and Qi (2001) showed that there are most likely 3 MAPRE genes: MAPRE1, which encodes EB1, MAPRE2 (605789), which encodes RP1 and the EB2 fragment, and MAPRE3 (605788), which encodes EBF3 and the fragment RP3.GENE FUNCTION
Berrueta et al. (1998) undertook a systematic study of EB1 subcellular localization during cell cycle, using both biochemical and immunofluorescence techniques. Using monoclonal antibodies specific for EB1, they demonstrated that EB1 decorated part of the microtubule cytoskeleton during interphase, with pronounced staining of the centrosome. During cell division, EB1 localized to the mitotic apparatus. This microtubule localization was abolished in the presence of the microtubule-destabilizing drug nocodazole; upon drug removal, the microtubule distribution of EB1 was recovered and EB1 fluorescence concentrated at the microtubule-organizing center. These results suggested that EB1 is associated with the microtubule network and may be involved in microtubule polymerization and spindle function. Associating with the mitotic apparatus, EB1 may play a physiologic role connecting APC to cell division, coordinating the control of normal growth and differentiation processes in the colonic epithelium. Tirnauer and Bierer (2000) reviewed the biology of EB1 family proteins. They noted that EB1 is a microtubule end-binding protein and that EB1 coimmunoprecipitates the dynactin components p150(GLUED) (DCTN1; 601143), p50/dynamitin (DCTN2; 607376), and the intermediate chain of dynein (see DNCI2; 603331) from lymphocytes and epithelial cells (Berrueta et al., 1999). By yeast 2-hybrid analysis of a HeLa cell cDNA library and pull-down assays using recombinant proteins, Sun et al. (2008) showed that the C-terminal tail of EB1 interacted specifically with the catalytic domain of Aurora kinase B (AURKB; 604970). The proteins colocalized on the central spindle in anaphase and in the midbody during cytokinesis in simian kidney cells, and endogenous EB1 and AURKB coimmunoprecipitated from HeLa cells. EB1 overexpression enhanced AURKB kinase activity, and knockdown of EB1 with small interfering RNA impaired AURKB activity. EB1 protected AURKB from dephosphorylation/inactivation by protein phosphatase-2A (PP2A; see 176915) by blocking binding of PP2A to AURKB. Sun et al. (2008) concluded that EB1 stimulates AURKB activity by antagonizing its dephosphorylation/inactivation by PP2A. Using U2OS human osteosarcoma cells, Tanenbaum et al. (2011) identified KIF18B (614570) as an essential component of a microtubule-depolymerizing complex containing MCAK (KIF2C; 604538) and EB1. KIF18B interacted independently with MCAK and a subset of EB1 at microtubule plus ends. All 3 proteins, in addition to KIF18B motor activity, were required ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 603108 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed