Gem-associated protein 5

Definition:

The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex. Binds to the 7-methylguanosine cap of RNA molecules. Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability. May play a role in the regulation of protein synthesis via its interaction with ribosomes.

References:

[1]. Daniel J Battle, et al. The Gemin5 protein of the SMN complex identifies snRNAs. Mol Cell. 2006 Jul 21;23(2):273-9. [Content Brief]

[2]. Xuhua Tang, et al. Structural basis for specific recognition of pre-snRNA by Gemin5. Cell Res. 2016 Dec;26(12):1353-1356. [Content Brief]

[3]. Sukhleen Kour, et al. Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder. Nat Commun. 2021 May 7;12(1):2558. [Content Brief]

[4]. Jeongsik Yong, et al. Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis. Mol Cell. 2010 May 28;38(4):551-62. [Content Brief]

[5]. Shelton S Bradrick, et al. Identification of gemin5 as a novel 7-methylguanosine cap-binding protein. PLoS One. 2009 Sep 14;4(9):e7030. [Content Brief]

[6]. Chao Xu, et al. Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly. Genes Dev. 2016 Nov 1;30(21):2376-2390. [Content Brief]

[7]. Wenxing Jin, et al. Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5. Genes Dev. 2016 Nov 1;30(21):2391-2403. [Content Brief]

[8]. Ashwin Chari, et al. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell. 2008 Oct 31;135(3):497-509. [Content Brief]

[9]. Eileen Workman, et al. Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate SMN Expression. J Biol Chem. 2015 Jun 19;290(25):15662-15669. [Content Brief]

[10]. Chi-kong Lau, et al. Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains. Nat Struct Mol Biol. 2009 May;16(5):486-91. [Content Brief]

[11]. Amelie K Gubitz, et al. Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins. J Biol Chem. 2002 Feb 15;277(7):5631-6. [Content Brief]

[12]. Rosario Francisco-Velilla, et al. The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation. Nucleic Acids Res. 2016 Sep 30;44(17):8335-51. [Content Brief]

[13]. Tracey J Golembe, et al. Specific sequence features, recognized by the SMN complex, identify snRNAs and determine their fate as snRNPs. Mol Cell Biol. 2005 Dec;25(24):10989-1004. [Content Brief]

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