Wikipedia

NDEL1

Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.[5][6][7]

NDEL1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNDEL1, EOPA, MITAP1, NDE1L1, NDE2, NUDEL, nudE neurodevelopment protein 1 like 1
External IDsOMIM: 607538; MGI: 1932915; HomoloGene: 32567; GeneCards: NDEL1; OMA:NDEL1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

81565

83431

Ensembl

ENSG00000166579

ENSMUSG00000018736

UniProt

Q9GZM8

Q9ERR1

RefSeq (mRNA)

NM_001025579
NM_030808
NM_001330129

NM_023668
NM_001363304
NM_001363305

RefSeq (protein)

NP_001020750
NP_001317058
NP_110435

NP_076157
NP_001350233
NP_001350234

Location (UCSC)Chr 17: 8.41 – 8.49 MbChr 11: 68.71 – 68.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[8] 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.[9][10][11] Nde1 and Ndel1 were in the past referred to as NudE and NudEL respectively.[12][13] The Nde1 protein is involved in nuclear migration throughout the process of neurogenesis.[14] Studies have revealed that Ndel1 is structurally similar to Nde1 which both play a role in microtubule-based transport.[8] Ndel1 and Nde1 are also thought to be associated with neurodevelopmental and psychiatric disorders.[14][15] 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.[16] 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.[16] 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.[13]

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.[7]

Other Interactions

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NDEL1 has been shown to interact with Cyclin-dependent kinase 5,[5] YWHAE,[17] PAFAH1B1[5][17] and DISC1.[18][19]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166579 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018736 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c Niethammer M, Smith DS, Ayala R, Peng J, Ko J, Lee MS, Morabito M, Tsai LH (Dec 2000). "NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein". Neuron. 28 (3): 697–711. doi:10.1016/S0896-6273(00)00147-1. PMID 11163260. S2CID 11154069.
  6. ^ Sasaki S, Shionoya A, Ishida M, Gambello MJ, Yingling J, Wynshaw-Boris A, Hirotsune S (Dec 2000). "A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing and adult nervous system". Neuron. 28 (3): 681–96. doi:10.1016/S0896-6273(00)00146-X. PMID 11163259. S2CID 17738599.
  7. ^ a b "Entrez Gene: NDEL1 nudE nuclear distribution gene E homolog (A. nidulans)-like 1".
  8. ^ a b 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): 104735. doi:10.1016/j.jbc.2023.104735. ISSN 0021-9258. PMC 10248797. PMID 37086789.
  9. ^ Sasaki, Shinji; Mori, Daisuke; Toyo-oka, Kazuhito; Chen, Amy; Garrett-Beal, Lisa; Muramatsu, Masami; Miyagawa, Shuji; Hiraiwa, Noriko; Yoshiki, Atsushi; Wynshaw-Boris, Anthony; Hirotsune, Shinji (2005-09-01). "Complete Loss of Ndel1 Results in Neuronal Migration Defects and Early Embryonic Lethality". Molecular and Cellular Biology. 25 (17): 7812–7827. doi:10.1128/MCB.25.17.7812-7827.2005. ISSN 1098-5549. PMC 1190282. PMID 16107726.
  10. ^ Shim, Su Yeon; Samuels, Benjamin Adam; Wang, Jian; Neumayer, Gernot; Belzil, Camille; Ayala, Ramses; Shi, Yang; Shi, Yujiang; Tsai, Li-Huei; Nguyen, Minh Dang (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.
  11. ^ 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.
  12. ^ 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. PMC 2881166. PMID 20403325.
  13. ^ a b 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. PMC 3101096. PMID 21282465.
  14. ^ a b 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. PMC 7775536. PMID 33390896.
  15. ^ Bradshaw, Nicholas J.; Hennah, William; Soares, Dinesh C. (2013-10-01). "NDE1 and NDEL1: twin neurodevelopmental proteins with similar 'nature' but different 'nurture'". BioMolecular Concepts. 4 (5): 447–464. doi:10.1515/bmc-2013-0023. ISSN 1868-503X. PMC 3787581. PMID 24093049.
  16. ^ a b Derewenda, Urszula; Tarricone, Cataldo; Choi, Won Chan; Cooper, David R.; Lukasik, Steve; Perrina, Franco; Tripathy, Ashutosh; Kim, Myung Hee; Cafiso, David S.; Musacchio, Andrea; Derewenda, Zygmunt S. (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.
  17. ^ a b Toyo-oka K, Shionoya A, Gambello MJ, Cardoso C, Leventer R, Ward HL, Ayala R, Tsai LH, Dobyns W, Ledbetter D, Hirotsune S, Wynshaw-Boris A (Jul 2003). "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. doi:10.1038/ng1169. PMID 12796778. S2CID 10301633.
  18. ^ Morris JA, Kandpal G, Ma L, Austin CP (Jul 2003). "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. doi:10.1093/hmg/ddg162. PMID 12812986.
  19. ^ Ozeki Y, Tomoda T, Kleiderlein J, Kamiya A, Bord L, Fujii K, Okawa M, Yamada N, Hatten ME, Snyder SH, Ross CA, Sawa A (Jan 2003). "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. Bibcode:2003PNAS..100..289O. doi:10.1073/pnas.0136913100. PMC 140954. PMID 12506198.

Further reading

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