Abstract
Serine-threonine kinase receptor-associated protein (STRAP) functions as a regulator of both TGF-β and p53 signaling that participates in the regulation of cell proliferation and cell death in response to various stresses. Here, we demonstrate that STRAP acetylation plays an important role in p53-mediated cell cycle arrest and apoptosis. STRAP is acetylated at lysines 147, 148, and 156 by the acetyltransferases CREB-binding protein (CBP) and that the acetylation is reversed by the deacetylase sirtuin7 (SIRT7). Hypo- or hyperacetylation mutations of STRAP at lysines 147, 148, and 156 (3KR or 3KQ) influence its activation and stabilization of p53. Moreover, following 5-fluorouracil (5-FU) treatment, STRAP is mobilized from the cytoplasm to the nucleus and promotes STRAP acetylation. Our finding on the regulation of STRAP links p53 with SIRT7 influencing p53 activity and stability.
Highlights
Serine/threonine kinase receptor associated protein (STRAP), known as the transforming growth factor-β1 (TGF-β) signaling negative regulator protein, is a 38kD protein that contains a WD40 domain [1]
The results showed that SIRT7 can interact with STRAP (Figure 1A), and vice versa (Figure 1B)
STRAP is mainly present in the cytoplasm, and SIRT7 is mainly present in the nucleus
Summary
Serine/threonine kinase receptor associated protein (STRAP), known as the transforming growth factor-β1 (TGF-β) signaling negative regulator protein, is a 38kD protein that contains a WD40 domain [1]. It has been reported that STRAP binds to SMAD family member 7 (Smad7) and synergistically inhibits downstream signaling of TGF-β receptors, as a negative regulator of the TGF-β pathway [4]. STRAP has been found to directly interact with p53 to enhance p53-induced apoptosis [13]. These reports indicate that STRAP might play a dual role in cellular processes.
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