Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2

Abstract

Alternative splicing patterns are regulated by RNA binding proteins that assemble onto each pre-mRNA to form a complex RNP structure. The polypyrimidine tract binding protein, PTB, has served as an informative model for understanding how RNA binding proteins affect spliceosome assembly and how changes in the expression of these proteins can control complex programs of splicing in tissues. In this review, we describe the mechanisms of splicing regulation by PTB and its function, along with its paralog PTBP2, in neuronal development.

Keywords::

• Alternative splicing
• spliceosome
• RNA binding protein
• neuronal development
• RNP

Acknowledgements

We thank our many colleagues in the PTB field for illuminating discussions and our anonymous reviewers for helpful corrections to the manuscript. We apologize for unreferenced important results.

Declaration of interest

Our own work has been supported by NIH Grants RO1 GM49662, R24 GM070857 (to D.L.B.), fellowship and training grant support from an NRSA and 5T32 NS07449 (to N.K.) and from NARSAD (to Q.L.), a grant from the California Institute for Regenerative Medicine (RFA 09-02), and funding from the Howard Hughes Medical Institute. D.L.B. is an investigator of the HHMI. We declare no financial interests in any of the work described.

Editor: Michael M. Cox