Sandbox Reserved 718
From Proteopedia
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Lin28 is a conserved cytoplasmic protein with an unusual pairing of RNA‑binding motifs: a cold shock domain and a pair of retroviral‑type CCHC zinc fingers. | Lin28 is a conserved cytoplasmic protein with an unusual pairing of RNA‑binding motifs: a cold shock domain and a pair of retroviral‑type CCHC zinc fingers. | ||
- | + | Lin28 is a conserved cytoplasmic protein with an unusual pairing of RNA binding motifs: a cold shock domain and a pair of retroviral type CCHC zinc fingers. It plays a critical role in developmental transition, glucose metabolism, and tumorigenesis. At the molecular level, LIN28 is known to repress maturation of let-7 microRNAs and enhance translation of certain mRNAs. Mammals have two homologs, Lin28a and Lin28b. These two homologs are found from worms to humans (Cho et al., 2012, Balzer and Moss, 2007). Lin28a is highly expressed in embryonic stem cells (ESCs) and was shown as one of the four factors that convert fibroblasts into induced pluripotent stem cells (Yu et al., 2007). | |
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== '''Structure''' == | == '''Structure''' == |
Revision as of 17:34, 1 January 2013
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Lin28 is a conserved cytoplasmic protein with an unusual pairing of RNA‑binding motifs: a cold shock domain and a pair of retroviral‑type CCHC zinc fingers.
Lin28 is a conserved cytoplasmic protein with an unusual pairing of RNA binding motifs: a cold shock domain and a pair of retroviral type CCHC zinc fingers. It plays a critical role in developmental transition, glucose metabolism, and tumorigenesis. At the molecular level, LIN28 is known to repress maturation of let-7 microRNAs and enhance translation of certain mRNAs. Mammals have two homologs, Lin28a and Lin28b. These two homologs are found from worms to humans (Cho et al., 2012, Balzer and Moss, 2007). Lin28a is highly expressed in embryonic stem cells (ESCs) and was shown as one of the four factors that convert fibroblasts into induced pluripotent stem cells (Yu et al., 2007).
Contents |
Structure
Applications
References
Contributors
Katrin Frohnmüller, Teresa Wiese
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