[4][5][6] Many RBPs have modular structures and are composed of multiple repeats of just a few specific basic domains that often have limited sequences.

It is a regulatory mechanism by which variations in the incorporation of the exons into mRNA leads to the production of more than one related protein, thus expanding possible genomic outputs.

The splicesome is a complex of snRNA and protein subunits and acts as the mechanical agent that removes introns and ligates the flanking exons.

[7] Other than core splicesome complex, RBPs also bind to the sites of Cis-acting RNA elements that influence exons inclusion or exclusion during splicing.

This process effectively changes the RNA sequence from that encoded by the genome and extends the diversity of the gene products.

[5] Polyadenylation is the addition of a "tail" of adenylate residues to an RNA transcript about 20 bases downstream of the AAUAAA sequence within the three prime untranslated region.

[9] More recent studies of FMRP-bound RNAs present in microdissected dendrites of CA1 hippocampal neurons revealed no changes in localization in wild type versus FMRP-null mouse brains.

[11] Specific binding of the RNA-binding proteins allow them to distinguish their targets and regulate a variety of cellular functions via control of the generation, maturation, and lifespan of the RNA transcript.

[12] Cross-linking immunoprecipitation (CLIP) methods are used to stringently identify direct RNA binding sites of RNA-binding proteins in a variety of tissues and organisms.

All RRMs' main protein surfaces' four-stranded β-sheet was found to interact with the RNA, which usually contacts two or three nucleotides in a specific manner.

All three structures of the domain solved as of 2005 possess uniting features that explain how dsRMs only bind to dsRNA instead of dsDNA.

Furthermore, the interaction between protein side-chains of the α-helix with the DNA bases in the major groove allows for the DNA-sequence-specific recognition.

[13] Extensive research on the nematode C. elegans has identified RNA-binding proteins as essential factors during germline and early embryonic development.

Their specific function involves the development of somatic tissues (neurons, hypodermis, muscles and excretory cells) as well as providing timing cues for the developmental events.

Nevertheless, it is exceptionally challenging to discover the mechanism behind RBPs' function in development due to the difficulty in identifying their RNA targets.

In Drosophila melanogaster, Elav, Sxl and tra-2 are RNA-binding protein encoding genes that are critical in the early sex determination and the maintenance of the somatic sexual state.

[14] Furthermore, another RRM-containing RBP, EXC-7, is revealed to localize in embryonic excretory canal cells and throughout the nervous system during somatic development.

[16] Other RNA-binding proteins involved in dendrite formation are Pumilio and Nanos,[17] FMRP, CPEB and Staufen 1[18] RBPs are emerging to play a crucial role in tumor development.

[19] Hundreds of RBPs are markedly dysregulated across human cancers and showed predominant downregulation in tumors related to normal tissues.

[26][30][31] As RNA-binding proteins exert significant control over numerous cellular functions, they have been a popular area of investigation for many researchers.

Due to its importance in the biological field, numerous discoveries regarding RNA-binding proteins' potentials have been recently unveiled.

Loss of Sam68 results in abnormal posttranscriptional regulation and ultimately leads to neurological disorders such as fragile X-associated tremor/ataxia syndrome.

Sam68 was found to interact with the mRNA encoding β-actin, which regulates the synaptic formation of the dendritic spines with its cytoskeletal components.

[35] Neuron-specific CELF family RNA-binding protein UNC-75 specifically binds to the UUGUUGUGUUGU mRNA stretch via its three RNA recognition motifs for the exon 7a selection in C. elegans' neuronal cells.

[37] Serine-arginine family of RNA-binding protein Slr1 was found exert control on the polarized growth in Candida albicans.

Slr1 mutations in mice results in decreased filamentation and reduces damage to epithelial and endothelial cells that leads to extended survival rate compared to the Slr1 wild-type strains.