Phosphorylated HuR shuttles in cycles

• Published in: Cell cycle (Georgetown, Tex.) Vol. 7; no. 20; pp. 3124 - 3126
• Main Authors: Kim, Hyeon Ho, Gorospe, Myriam
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 15.10.2008
• Subjects: Active Transport, Cell Nucleus - physiology; Amino Acid Sequence; Animals; Antigens, Surface - chemistry; Antigens, Surface - genetics; Antigens, Surface - metabolism; Binding; Biology; Bioscience; Calcium; Cancer; Cell; Cell Cycle - physiology; Cycle; Cyclins - metabolism; Cytoplasm - metabolism; ELAV Proteins; ELAV-Like Protein 1; Extra View; Humans; Landes; Molecular Sequence Data; Organogenesis; Phosphorylation; Protein Kinase C - metabolism; Proteins; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism
• ISSN: 1538-4101; 1551-4005
• DOI: 10.4161/cc.7.20.6884

HuR is a ubiquitous RNA-binding protein (RBP) that associates with many mRNAs encoding proliferative proteins. Although predominantly nuclear, HuR translocation to the cytoplasm is linked to its ability to stabilize target mRNAs and modulate their translation. We recently reported that HuR phosphorylation by Cdk1 at S202 (within the HuR hinge region that is necessary for nucleocytoplasmic shuttle) increases HuR association with 14-3-3 and contributes to its nuclear retention. In this issue of Cell Cycle we report that residue S242 also regulates HuRâÃ,€Ã,™s cytoplasmic localization, influences cyclin expression, and modulates cell proliferation. Together with evidence of other post-translational HuR modifications, we propose that HuR phosphorylation ensures the timely mobilization of HuR across the nuclear envelope. In turn, HuR helps to schedule gene expression programs in a cell cycle-dependent manner.