Ltv1 and Its Role in Protein Trafficking and Ribosomal Assembly in Saccharomyces cerevisiae

Abstract

In Saccharomyces cerevisiae, ltv1 is involved in assembling and trafficking the 40S subunit in ribosomes, as well as trafficking other proteins such as GAP1p. LTV1p helps facilitate 40S subunit assembly by binding ENP1p and recruiting other proteins. After, nuclear export of the 40S subunit occurs via the leucine-rich nuclear export signal (NES). The formation of ribosomes is essential for protein synthesis, therefore, mutating ltv1 has many physiological consequences. Several studies have reported that the deletion mutant, ltv1-Δ affects growth, sensitivity to stressors and ribosomal assembly and production in S. cerevisiae. This review summarizes current findings on the ltv1 gene, LTV1p protein structure and function, as well as the consequences of ltv1 knockout mutation. Although ltv1 is involved in several molecular pathways, the involvement of ltv1 in plasma membrane recycling and 40S subunit assembly is not fully understood. It is also unknown how ltv1-Δ mutants respond to stressors such as changes in pH and increased temperature. Therefore, this review proposes a mechanism for how ltv1 is involved in pre-40S subunit assembly and suggests what type of research can be done to broaden our understanding of the ltv1 gene.