MARCKSL1

MARCKSL1
Identifiers
Aliases	MARCKSL1 , F52, MACMARCKS, MLP, MLP1, MRP, MARCKS-like 1, MARCKS like 1
External IDs	OMIM: 602940; MGI: 97143; HomoloGene: 40748; GeneCards: MARCKSL1; OMA:MARCKSL1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p35.1 Start 32,333,839 bp [1] End 32,336,233 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4 D2.2|4 63.26 cM Start 129,407,374 bp [2] End 129,409,778 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior ganglion of vagus nerve ganglionic eminence spinal cord C1 segment superior vestibular nucleus middle frontal gyrus subthalamic nucleus Pons ventricular zone ventral tegmental area Top expressed in neural tube maxillary prominence medial ganglionic eminence mandibular prominence somite abdominal wall ventricular zone primitive streak transitional epithelium of urinary bladder vestibular sensory epithelium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function actin binding protein binding calmodulin binding Cellular component cytoplasm plasma membrane extracellular exosome membrane cytoskeleton Biological process positive regulation of cell population proliferation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 65108 17357 Ensembl ENSG00000175130 ENSMUSG00000047945 UniProt P49006 P28667 RefSeq (mRNA) NM_023009 NM_010807 RefSeq (protein) NP_075385 NP_034937 Location (UCSC) Chr 1: 32.33 – 32.34 Mb Chr 4: 129.41 – 129.41 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

MARCKS-related protein is a protein that in humans is encoded by the MARCKSL1 gene. ^{[5] [6]}

Function

This gene encodes a member of the myristoylated alanine-rich C-kinase substrate (MARCKS) family. MARCKS plays a role in cytoskeletal regulation, protein kinase C signaling and calmodulin signaling. The encoded protein affects the formation of adherens junctions. Alternative splicing results in multiple transcript variants. ^[6]

Interactions

MARCKSL1 has been shown to interact with DCTN2 ^[7] and JNK. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000175130 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000047945 – 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. Stumpo DJ, Eddy RL, Haley LL, Sait S, Shows TB, Lai WS, Young WS, Speer MC, Dehejia A, Polymeropoulos M, Blackshear PJ (August 1998). "Promoter sequence, expression, and fine chromosomal mapping of the human gene (MLP) encoding the MARCKS-like protein: identification of neighboring and linked polymorphic loci for MLP and MACS and use in the evaluation of human neural tube defects". Genomics. 49 (2): 253–64. doi:10.1006/geno.1998.5247. PMID   9598313.
6. "Entrez Gene: MARCKSL1 MARCKS-like 1".
7. Yue L, Lu S, Garces J, Jin T, Li J (August 2000). "Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated alanine-rice C kinase substrate interaction is involved in macrophage cell spreading". J. Biol. Chem. 275 (31): 23948–56. doi: 10.1074/jbc.M001845200 . PMID   10827182.
8. Björkblom B, Padzik A, Mohammad H, Westerlund N, Komulainen E, Hollos P, Parviainen L, Papageorgiou AC, Iljin K, Kallioniemi O, Kallajoki M, Courtney MJ, Mågård M, James P, Coffey ET (September 2012). "c-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cells". Mol Cell Biol. 32 (17): 3513–26. doi:10.1128/MCB.00713-12. PMC   3421996 . PMID   22751924.

Further reading

• Umekage T, Kato K (1991). "A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS". FEBS Lett. 286 (1–2): 147–51. doi: 10.1016/0014-5793(91)80961-2 . PMID   1864362.
• Verghese GM, Johnson JD, Vasulka C, Haupt DM, Stumpo DJ, Blackshear PJ (1994). "Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein". J. Biol. Chem. 269 (12): 9361–7. doi: 10.1016/S0021-9258(17)37116-8 . PMID   8132675.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID   8619474.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC   139146 . PMID   9110174.
• Yue L, Lu S, Garces J, Jin T, Li J (2000). "Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated alanine-rice C kinase substrate interaction is involved in macrophage cell spreading". J. Biol. Chem. 275 (31): 23948–56. doi: 10.1074/jbc.M001845200 . PMID   10827182.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC   310948 . PMID   11076863.
• Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC   1083732 . PMID   11256614.
• Hsia TC, Lin CC, Wang JJ, Ho ST, Kao A (2002). "Relationship between chemotherapy response of small cell lung cancer and P-glycoprotein or multidrug resistance-related protein expression". Lung. 180 (3): 173–9. doi:10.1007/s004080000091. PMID   12177731. S2CID   23345753.
• Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi: 10.1074/mcp.M400085-MCP200 . PMID   15345747.
• Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC   528930 . PMID   15489336.
• Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC   1347501 . PMID   16381901.
• Jordanova A, Irobi J, Thomas FP, Van Dijck P, Meerschaert K, Dewil M, Dierick I, Jacobs A, De Vriendt E, Guergueltcheva V, Rao CV, Tournev I, Gondim FA, D'Hooghe M, Van Gerwen V, Callaerts P, Van Den Bosch L, Timmermans JP, Robberecht W, Gettemans J, Thevelein JM, De Jonghe P, Kremensky I, Timmerman V (2006). "Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy" . Nat. Genet. 38 (2): 197–202. doi:10.1038/ng1727. PMID   16429158. S2CID   16668375.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983. S2CID   7827573.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.