A novel nuclear export signal in Smad1 is essential for its signaling activity.

TL;DR: The exquisite nature of TGF-β family signaling in its roles in diverse and context-specific cellular behaviors is described and the mechanisms through which proteins called Smads act as intracellular effectors of ligand-induced gene expression responses are introduced, showing that the specificity and impressive versatility of Smad signaling depend on cross-talk from other pathways.

TL;DR: In this article, the authors make an attempt to summarize the TGF-β-mediated SMAD-dependent and SMADindependent pathways and emphasize the functions of TGFβ as a metastatic promoter and tumor suppressor during the later and initial phases of tumor progression respectively.

TL;DR: This review makes an attempt to showcase the associated enigma of TGFβ signaling in its dual functional role as tumor suppressor and metastatic promoter during early and late stages of carcinogenesis, respectively.

TL;DR: The results indicate that the RK-rich region of SIK1 is important for determining the nuclear localization and attenuating CREB-repressing activity, but the degree of thenuclear localization of Sik1 itself does not necessarily reflect the degreeof SIK 1-mediated CREB repression.

TL;DR: TGF‐β family members are multifunctional hormones, the nature of their effects depending on what has been called ‘the cellular context’ warrants mention at the outset.

TL;DR: It is shown that M9 is also a nuclear export signal; placing M9 on a protein that is otherwise restricted to the nucleus, the nucleoplasmin core domain (NPc), efficiently exports it to the cytoplasm in a temperature-dependent manner.

TL;DR: It is demonstrated that NES activity is a defining characteristic of the activation domains found in the Rev/Rex class of retroviral regulatory proteins and strongly support the hypothesis that the Rab/hRIP cofactor plays a critical role in mediating the biological activity of these NESs.

TL;DR: It is suggested that MTs may serve as a cytoplasmic sequestering network for Smads, controlling Smad2 association with and phosphorylation by activated TGFβ receptor I, and suggest a novel mechanism for the MT network to negatively regulate TGF β function.