Biology:NDEL1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.[1][2][3]

It plays a significant role in intracellular transport and the process of cellular division via regulation of the dynein motor protein and its cofactor protein, Lis1.[4] Ndel1 is a highly conserved protein and its human gene, NDEL1 is expressed in a wide variety of brain tissues which contributes to neuronal function and development.[5][6][7] Nde1 and Ndel1 were in the past referred to as NudE and NudEL respectively.[8][9] The Nde1 protein is involved in nuclear migration throughout the process of neurogenesis.[10] Studies have revealed that Ndel1 is structurally similar to Nde1 which both play a role in microtubule-based transport.[4] Ndel1 and Nde1 are also thought to be associated with neurodevelopmental and psychiatric disorders.[10][11] Secondary structure of Ndel1 is composed of various distinct domains: a C-terminal region, and a 200 amino acid N-terminal coiled-coil domain. The coiled-coil domain of Ndel1 serves as a self-associating stable parallel homodimer.[12] Such structural components help with interactions between an array of binding partners, including the motor protein dynein and its cofactor protein, Lis1. Ndel1 forms a heterotetramer complex with Lis1 via the N-terminal coiled-coil domain.[12] The Ndel1 N-terminal coiled-coil domain mediates binding to dynein, whereas the C-terminal domain interacts with Lis1, regulating the activity of the dynein complex.[9]

This gene product is a thiol-activated oligopeptidase and is also known as Endooligopeptidase A in that context. It is phosphorylated in M phase of the cell cycle. Phosphorylation regulates the cell cycle-dependent distribution of this protein, with a fraction of the protein bound strongly to centrosomes in interphase and localized to mitotic spindles in early M phase. Overall, this protein plays a role in nervous system development. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[3]

Other Interactions

NDEL1 has been shown to interact with Cyclin-dependent kinase 5,[1] YWHAE,[13] PAFAH1B1[1][13] and DISC1.[14][15]

References

  1. ↑ 1.0 1.1 1.2 "NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein". Neuron 28 (3): 697–711. Dec 2000. doi:10.1016/S0896-6273(00)00147-1. PMID 11163260. 
  2. ↑ "A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing and adult nervous system". Neuron 28 (3): 681–96. Dec 2000. doi:10.1016/S0896-6273(00)00146-X. PMID 11163259. 
  3. ↑ 3.0 3.1 "Entrez Gene: NDEL1 nudE nuclear distribution gene E homolog (A. nidulans)-like 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=81565. 
  4. ↑ 4.0 4.1 Garrott, Sharon R.; Gillies, John P.; Siva, Aravintha; Little, Saffron R.; El Jbeily, Rita; DeSantis, Morgan E. (June 2023). "Ndel1 disfavors dynein–dynactin–adaptor complex formation in two distinct ways". Journal of Biological Chemistry 299 (6). doi:10.1016/j.jbc.2023.104735. ISSN 0021-9258. PMID 37086789. 
  5. ↑ Sasaki, Shinji; Mori, Daisuke; Toyo-oka, Kazuhito; Chen, Amy; Garrett-Beal, Lisa; Muramatsu, Masami; Miyagawa, Shuji; Hiraiwa, Noriko et al. (2005-09-01). "Complete Loss of Ndel1 Results in Neuronal Migration Defects and Early Embryonic Lethality" (in en). Molecular and Cellular Biology 25 (17): 7812–7827. doi:10.1128/MCB.25.17.7812-7827.2005. ISSN 1098-5549. PMID 16107726. 
  6. ↑ Shim, Su Yeon; Samuels, Benjamin Adam; Wang, Jian; Neumayer, Gernot; Belzil, Camille; Ayala, Ramses; Shi, Yang; Shi, Yujiang et al. (May 2008). "Ndel1 Controls the Dynein-mediated Transport of Vimentin during Neurite Outgrowth". Journal of Biological Chemistry 283 (18): 12232–12240. doi:10.1074/jbc.m710200200. ISSN 0021-9258. PMID 18303022. 
  7. ↑ Shu, Tianzhi; Ayala, Ramses; Nguyen, Minh-Dang; Xie, Zhigang; Gleeson, Joseph G.; Tsai, Li-Huei (October 2004). "Ndel1 Operates in a Common Pathway with LIS1 and Cytoplasmic Dynein to Regulate Cortical Neuronal Positioning". Neuron 44 (2): 263–277. doi:10.1016/j.neuron.2004.09.030. ISSN 0896-6273. PMID 15473966. 
  8. ↑ McKenney, Richard J.; Vershinin, Michael; Kunwar, Ambarish; Vallee, Richard B.; Gross, Steven P. (April 2010). "LIS1 and NudE Induce a Persistent Dynein Force-Producing State". Cell 141 (2): 304–314. doi:10.1016/j.cell.2010.02.035. ISSN 0092-8674. PMID 20403325. 
  9. ↑ 9.0 9.1 Żyłkiewicz, Eliza; Kijańska, Monika; Choi, Won-Chan; Derewenda, Urszula; Derewenda, Zygmunt S.; Stukenberg, P. Todd (2011-01-31). "The N-terminal coiled-coil of Ndel1 is a regulated scaffold that recruits LIS1 to dynein". Journal of Cell Biology 192 (3): 433–445. doi:10.1083/jcb.201011142. ISSN 1540-8140. PMID 21282465. 
  10. ↑ 10.0 10.1 Soto-Perez, Jaseph; Baumgartner, Marybeth; Kanadia, Rahul N. (2020). "Role of NDE1 in the Development and Evolution of the Gyrified Cortex". Frontiers in Neuroscience 14. doi:10.3389/fnins.2020.617513. ISSN 1662-453X. PMID 33390896. 
  11. ↑ Bradshaw, Nicholas J.; Hennah, William; Soares, Dinesh C. (2013-10-01). "NDE1 and NDEL1: twin neurodevelopmental proteins with similar 'nature' but different 'nurture'" (in en). BioMolecular Concepts 4 (5): 447–464. doi:10.1515/bmc-2013-0023. ISSN 1868-503X. PMID 24093049. 
  12. ↑ 12.0 12.1 Derewenda, Urszula; Tarricone, Cataldo; Choi, Won Chan; Cooper, David R.; Lukasik, Steve; Perrina, Franco; Tripathy, Ashutosh; Kim, Myung Hee et al. (November 2007). "The Structure of the Coiled-Coil Domain of Ndel1 and the Basis of Its Interaction with Lis1, the Causal Protein of Miller-Dieker Lissencephaly". Structure 15 (11): 1467–1481. doi:10.1016/j.str.2007.09.015. ISSN 0969-2126. PMID 17997972. 
  13. ↑ 13.0 13.1 "14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome". Nature Genetics 34 (3): 274–85. Jul 2003. doi:10.1038/ng1169. PMID 12796778. 
  14. ↑ "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation". Human Molecular Genetics 12 (13): 1591–608. Jul 2003. doi:10.1093/hmg/ddg162. PMID 12812986. 
  15. ↑ "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth". Proceedings of the National Academy of Sciences of the United States of America 100 (1): 289–94. Jan 2003. doi:10.1073/pnas.0136913100. PMID 12506198. Bibcode: 2003PNAS..100..289O. 

Further reading



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