Musashi-1, an RNA-binding protein, is indispensable for survival of photoreceptors

Susaki, Kanako; Kaneko, Jun; Yamano, Yuka; Nakamura, Kenta; Inami, Wataru; Yoshikawa, Taro; Ozawa, Yoko; Shibata, Shinsuke; Matsuzaki, Osamu; Chiba, Chikafumi

doi:10.1016/j.exer.2008.06.019

Cited by 39 publications

(44 citation statements)

References 24 publications

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“…In addition, we have confirmed a reduction in the levels of four other proteins unrelated to phototransduction function, but all of which have been linked to retinal degeneration. They include peripherin 2 and Rom1, which are critically involved in outer segment membrane morphogenesis and maintenance (25,26), along with synaptic protein Unc-119 (27) and RNA-binding protein musashi-1 (28). These data confirm the crucial role of the PhLP-CCT-assisted biosynthetic pathway in the folding and assembly of heterotrimeric G proteins, and additionally suggest that other components of the G protein signaling pathway may require CCT assistance for their biogenesis.…”

Section: Phlp-cct Deficiency Severely Affects the Phototransduction Psupporting

confidence: 60%

Disruption of the Chaperonin Containing TCP-1 Function Affects Protein Networks Essential for Rod Outer Segment Morphogenesis and Survival

Posokhova¹,

Song²,

Belcastro³

et al. 2011

Molecular & Cellular Proteomics

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Normal cellular function is hinged upon the ability of the endogenous machinery to properly process newly synthesized proteins, and this is often required for enabling their functional activity. Eukaryotic cells contain several proteinfolding, or chaperone, systems assisting in this process. Despite the apparent redundancy, it is believed that each chaperone system plays an important and unique role in facilitating protein folding by acting on distinct sets of substrates at unique cellular locations and/or under certain conditions (1, 2). One such chaperone system, unique to eukaryotic cells, is the Chaperonin Containing TCP-1 (CCT), 1 also known as TCP-1 Ring Complex (TRiC) (for reviews see 3, 1). CCT is composed of eight different subunits that assemble into a double ring structure, creating an internal cavity that serves as a folding chamber. A pioneering study demonstrated refolding of phytochrome, a light-sensing protein of plants, by a cytosolic molecular chaperone related to CCT (4). Studies in yeast and model mammalian cell lines indicate that the action of the CCT chaperonin is critical for cellular function. It is estimated that CCT may assist folding and assembly of up to 10% of all cellular proteins (5). Several recent studies reported identification of CCT substrates by proteomic and genetic methods (6, 7). Despite the important advances, these identified substrates are rather limited in number, and the set of the proteins requiring CCT assistance is likely to vary substantially across different specialized cells. Furthermore, virtually nothing is known about the involvement of the CCT chaperonin system in the regulation of specific cellular processes in the in vivo setting of complex multicellular organisms.Recent studies have established that the CCT function is regulated by phosducin-like proteins (PhLP) that are increasingly viewed as CCT co-chaperones (8). The best studied member of this family, PhLP, has been shown to be indispensable for the folding of the ␤ subunits of heterotrimeric G proteins that share a common WD40 motif with many CCT substrates (see ref. in 9). PhLP forms stable stoichiometric

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Section: Phlp-cct Deficiency Severely Affects the Phototransduction Psupporting

confidence: 60%

Disruption of the Chaperonin Containing TCP-1 Function Affects Protein Networks Essential for Rod Outer Segment Morphogenesis and Survival

Posokhova¹,

Song²,

Belcastro³

et al. 2011

Molecular & Cellular Proteomics

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“…Raji et al showed that Msi1 is produced in mouse eyes from embryonic stages until adulthood, and is also expressed in several unexpected sites, including the corneal epithelium and endothelium, stromal keratocytes, progenitor cells of the limbus, equatorial lens stem cells, differentiated lens epithelial cells, and differentiated lens fibers (20). A later study indicated that Msi1 knockout results in degeneration of photoreceptors and loss of visual cycle protein RPE65 in the microvilli of retinal pigment epithelium cells, which express Msi1 protein in wild-type animals (40). This could imply that Msi1 has an essential function for vision.…”

Section: Somatic Stem Cells and Msi1 Protein Functionmentioning

confidence: 96%

The Musashi family RNA-binding proteins in stem cells

Horisawa

Imai

Yanagawa

2010

BioMolecular Concepts

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The Musashi family is an evolutionarily conserved group of RNA-binding proteins. In mammal, two members of the group, Msi1 and Msi2, have been identified to date. Msi1 is considered to play roles in maintaining the stem cell status (stemness) of neural stem/progenitor cells in adults and in the development of central nervous system through translational regulation of its target mRNAs, which encode regulators of signal transduction and the cell cycle. Recently, strong expression of Msi1 in various somatic stem/progenitor cells of adult tissues, such as eye, gut, stomach, breast, and hair follicle, has been reported. The protein is also expressed in various cancer cells, and ectopically emerging cells have been found in neural tissues of patients with diseases involving neural disorder, including epilepsy. Many novel target mRNAs and regulatory pathways of Msi1 have been reported in recent years. Here, we present a review of the functions and action mechanisms of Msi1 protein and discuss possible directions for further study.

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“…Msi1, a multifunction RNA binding protein of MSI family, is present in many types of normal cells (27)(28)(29) and is involved in CNS stem/progenitor cell fate (13,30), inner ear development (31), repair of small-intestinal and stomach injury (32,33), and maturation of photoreceptor and oocyte (34,35), intestinal metaplasia (36), atherosclerotic arteries (37) and Alzheimer disease and Pick disease (38). Its overexpression in tumor cells promotes tumor growth, invasion and metastasis, inhibits apoptosis and predicts poor prognosis.…”

Section: Discussionmentioning

confidence: 99%

Downregulation of Msi1 suppresses the growth of human colon cancer by targeting p21cip1

Gao¹,

Han²,

Yu³

et al. 2014

International Journal of Oncology

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Abstract. Musashi1 (Msi1), a member of the RNA-binding protein (RBP) family, is highly expressed in neural progenitor or stem cells for the maintenance of stemness as well as in various cancers. Emerging studies have demonstrated that it regulates cell processes by translational activation or suppresses specifically bound mRNA. In the present study, we initially reported remarkably increased expression of Msi1 in colon cancer tissues compared with adjacent nontumor tissues. Knockdown of Msi1 significantly suppressed the proliferation, colony formation, tumorsphere formation and the progression of implanted colon cancers, and induced cell cycle attest at G 0 /G 1 phase, along with the upregulated expression of p21 cip1 . Reporter assays using a chimeric mRNA that combined luciferase and the 3'-UTR of p21 cip1 revealed that Msi1 decreased the reporter activity through the specific motif. Thus, the current results suggested that downregulation of Msi1 could inhibit the growth of colon cancers and Msi1 may be a promising therapeutic target molecule for human colon cancers.

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Musashi-1, an RNA-binding protein, is indispensable for survival of photoreceptors

Cited by 39 publications

References 24 publications

Disruption of the Chaperonin Containing TCP-1 Function Affects Protein Networks Essential for Rod Outer Segment Morphogenesis and Survival

Disruption of the Chaperonin Containing TCP-1 Function Affects Protein Networks Essential for Rod Outer Segment Morphogenesis and Survival

The Musashi family RNA-binding proteins in stem cells

Downregulation of Msi1 suppresses the growth of human colon cancer by targeting p21cip1

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