Cpc2/RACK1 Is a Ribosome-associated Protein That Promotes Efficient Translation in Schizosaccharomyces pombe

Shor, Boris; Calaycay, Jimmy; Rushbrook, Julie Ivory; McLeod, Maureen

doi:10.1074/jbc.m303968200

Cited by 75 publications

(94 citation statements)

References 59 publications

(59 reference statements)

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“…RACK1 has been shown to interact with a number of different signalling molecules, such as Src, intergrin-b and PKC, and through this interaction is thought to mediate translation regulation. In yeast RACK1 has been found to control translation initiation in an mRNA specific manner and is present in the cell in differently modified forms (Shor et al, 2003). This latter point is supported by our identification of RACK1 in multiple distinct spots with varying pI values but similar molecular masses.…”

Section: Discussionsupporting

confidence: 71%

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

et al. 2005

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Proteomic studies have addressed the composition of plant chloroplast ribosomes and 70S ribosomes from the unicellular organism Chlamydomonas reinhardtii, but comprehensive characterization of cytoplasmic 80S ribosomes from higher plants has been lacking. We have used two-dimensional gel electrophoresis (2-DE) and mass spectrometry (MS) to analyse the cytoplasmic 80S ribosomes from the model flowering plant Arabidopsis thaliana. Of the 80 ribosomal protein families predicted to comprise the cytoplasmic 80S ribosome, we have confirmed the presence of 61; specifically, 27 (84%) of the small 40S subunit and 34 (71%) of the large 60S subunit. Nearly half (45%) of the ribosomal proteins identified are represented by two or more distinct spots in the 2-DE gel indicating that these proteins are either post-translationally modified or present as different isoforms. Consistently, MS-based protein identification revealed that at least one-third (34%) of the identified ribosomal protein families showed expression of two or more family members. In addition, we have identified a number of non-ribosomal proteins that co-migrate with the plant 80S ribosomes during gradient centrifugation suggesting their possible association with the 80S ribosomes. Among them, RACK1 has recently been proposed to be a ribosome-associated protein that promotes efficient translation in yeast. The study, thus provides the basis for further investigation into the function of the other identified non-ribosomal proteins as well as the biological meaning of the various ribosomal protein isoforms.

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Section: Discussionsupporting

confidence: 71%

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

et al. 2005

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“…In agreement with this hypothesis, RACK1 is not an essential gene in yeast. RACK1 yeast mutants are viable 63 and show a slight impairment in the translation of a specific subset of mRNAs 64 unless challenged with stress. 25,63 …”

Section: Monographsmentioning

confidence: 99%

RACK1 Function in Cell Motility and Protein Synthesis

et al. 2013

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The receptor for activated C kinase 1 (RACK1) serves as an adaptor for a number of proteins along the MAPK, protein kinase C, and Src signaling pathways. The abundance and near ubiquitous expression of RACK1 reflect its role in coordinating signaling molecules for many critical biological processes, from mRNA translation to cell motility to cell survival and death. Complete deficiency of Rack1 is embryonic lethal, but the recent development of genetic Rack1 hypomorphic mice has highlighted the central role that RACK1 plays in cell movement and protein synthesis. This review focuses on the importance of RACK1 in these processes and places the recent work in the larger context of understanding RACK1 function.

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“…The S. pombe Cpc2/RACK1 homolog is required for efficient translation, cell cycle progression, and meiotic development of the cell (63,64). The high sequence similarity shared between Gib2 and Asc1/Cpc2/RACK1 could suggest that Gib2 has functions similar to these proteins.…”

Section: Discussionmentioning

confidence: 99%

Gib2, A Novel Gβ-like/RACK1 Homolog, Functions as a Gβ Subunit in cAMP Signaling and Is Essential in Cryptococcus neoformans

Palmer

Thompson

et al. 2006

Journal of Biological Chemistry

125

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Canonical G proteins are heterotrimeric, consisting of ␣, ␤, and ␥ subunits. Despite multiple G␣ subunits functioning in fungi, only a single G␤ subunit per species has been identified, suggesting that non-conventional G protein signaling exists in this diverse group of eukaryotic organisms. Using the G␣ subunit Gpa1 that functions in cAMP signaling as bait in a twohybrid screen, we have identified a novel G␤-like/RACK1 protein homolog, Gib2, from the human pathogenic fungus Cryptococcus neoformans. Gib2 contains a seven WD-40 repeat motif and is predicted to form a seven-bladed ␤ propeller structure characteristic of ␤ transducins. Gib2 is also shown to interact, respectively, with two G␥ subunit homologs, Gpg1 and Gpg2, similar to the conventional G␤ subunit Gpb1. In contrast to Gpb1 whose overexpression promotes mating response, overproduction of Gib2 suppresses defects of gpa1 mutation in both melanization and capsule formation, the phenotypes regulated by cAMP signaling and associated with virulence. Furthermore, depletion of Gib2 by antisense suppression results in a severe growth defect, suggesting that Gib2 is essential. Finally, Gib2 is shown to also physically interact with a downstream target of Gpa1-cAMP signaling, Smg1, and the protein kinase C homolog Pkc1, indicating that Gib2 is also a multifunctional RACK1-like protein.

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Cpc2/RACK1 Is a Ribosome-associated Protein That Promotes Efficient Translation in Schizosaccharomyces pombe

Cited by 75 publications

References 59 publications

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

RACK1 Function in Cell Motility and Protein Synthesis

Gib2, A Novel Gβ-like/RACK1 Homolog, Functions as a Gβ Subunit in cAMP Signaling and Is Essential in Cryptococcus neoformans

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