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Alimenti, K.

Publications and source records attributed to Alimenti, K..

2 recordsLinked to original sources

SAF-A/HNRNPU regulates euchromatin dynamics and is required for nuclear envelope integrity

Defects in nuclear morphology are associated with cancer and premature ageing. Nuclear morphology is established by a balance of external forces produced by actin contractility and resistance provided by chromatin and the nuclear lamina. Euchromatin is decompacted to facilitate transcription, which has been shown to decrease local nucleosome motion. However, the role of transcription and euchromatic chromatin structure in nuclear envelope integrity are not clear. Here, we demonstrate that acute depletion of SAF- A/hnRNPU causes compaction of euchromatic regions and constriction of chromatin mobility, leading to loss of nuclear envelope integrity in a transcription-dependent manner. SAF-A is required in a dose-dependent manner to preserve nuclear shape under conditions of nuclear softening and elevated transcription. Our work identifies SAF-A as a dynamic scaffold that regulates chromatin structure and dynamics at sites of active transcription to preserve nuclear envelope mechanical tension.

cell biology↗

Role of the SAF-A SAP domain in X inactivation, transcription, splicing, and cell proliferation

SAF-A is conserved throughout vertebrates and has emerged as an important factor regulating a multitude of nuclear functions, including lncRNA localization, gene expression, and splicing. SAF-A has several functional domains, including an N-terminal SAP domain that binds directly to DNA. Phosphorylation of SAP domain serines S14 and S26 are important for SAF-A localization and function during mitosis, however whether these serines are involved in interphase functions of SAF-A is not known. In this study we tested for the role of the SAP domain, and SAP domain serines S14 and S26 in X chromosome inactivation, protein dynamics, gene expression, splicing, and cell proliferation. Here we show that the SAP domain serines S14 and S26 are required to maintain XIST RNA localization and polycomb-dependent histone modifications on the inactive X chromosome in female cells. In addition, we present evidence that an Xi localization signal resides in the SAP domain. We found that that the SAP domain is not required to maintain gene expression and plays only a minor role in mRNA splicing. In contrast, the SAF-A SAP domain, in particular serines S14 and S26, are required for normal protein dynamics, and to maintain normal cell proliferation. We propose a model whereby dynamic phosphorylation of SAF-A serines S14 and S26 mediates rapid turnover of SAF-A interactions with DNA during interphase.

cell biology↗