The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL. Supplemental Materials
نویسندگان
چکیده
Title The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL Author(s) Mannen, Taro; Yamashita, Seisuke; Tomita, Kozo; Goshima, Naoki; Hirose, Tetsuro Citation Journal of cell biology, 214(1): 45-59 Issue Date 2016-07-04 Doc URL http://hdl.handle.net/2115/62689 Right ©Mannen et al., 2016. Originally published in the journal of cell biology. doi:10.1083/jcb.201601024
منابع مشابه
The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL
The mammalian cell nucleus contains membraneless suborganelles referred to as nuclear bodies (NBs). Some NBs are formed with an architectural RNA (arcRNA) as the structural core. Here, we searched for new NBs that are built on unidentified arcRNAs by screening for ribonuclease (RNase)-sensitive NBs using 32,651 fluorescently tagged human cDNA clones. We identified 32 tagged proteins that requir...
متن کاملIdentification of a Sam68 ribonucleoprotein complex regulated by epidermal growth factor.
Sam68, Src associated in mitosis of 68 kDa, is a known RNA-binding protein and a signaling adaptor protein for tyrosine kinases. However, the proteins associated with Sam68 and the existence of a Sam68 complex, its mass, and regulation are, however, unknown. Herein we identify a large Sam68 complex with a mass >1 MDa in HeLa cells that is composed of approximately 40 proteins using an immunopre...
متن کاملAn adaptor role for cytoplasmic Sam68 in modulating Src activity during cell polarization.
The Src-associated substrate during mitosis with a molecular mass of 68 kDa (Sam68) is predominantly nuclear and is known to associate with proteins containing the Src homology 3 (SH3) and SH2 domains. Although Sam68 is a Src substrate, little is known about the signaling pathway that link them. Src is known to be activated transiently after cell spreading, where it modulates the activity of sm...
متن کاملA role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cell lines.
The GSG (GRP33, Sam68, GLD-1) domain is a protein module found in an expanding family of RNA-binding proteins. The numerous missense mutations identified genetically in the GSG domain support its physiological role. Although the exact function of the GSG domain is not known, it has been shown to be required for RNA binding and oligomerization. Here it is shown that the Sam68 GSG domain plays a ...
متن کاملWhole-genome screening identifies proteins localized to distinct nuclear bodies
The nucleus is a unique organelle that contains essential genetic materials in chromosome territories. The interchromatin space is composed of nuclear subcompartments, which are defined by several distinctive nuclear bodies believed to be factories of DNA or RNA processing and sites of transcriptional and/or posttranscriptional regulation. In this paper, we performed a genome-wide microscopy-ba...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2017