MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin.
نویسندگان
چکیده
The "MAN antigens" are polypeptides recognized by autoantibodies from a patient with a collagen vascular disease and localized to the nuclear envelope. We now show that one of the human MAN antigens termed MAN1 is a 82.3-kDa protein with an amino-terminal domain followed by two hydrophobic segments and a carboxyl-terminal tail. The MAN1 gene contains seven protein-coding exons and is assigned to human chromosome 12q14. Its mRNA is approximately 5.5 kilobases and is detected in several different cell types that were examined. Cell extraction experiments show that MAN1 is an integral membrane protein. When expressed in transfected cells, MAN1 is exclusively targeted to the nuclear envelope, consistent with an inner nuclear membrane localization. Protein sequence analysis reveals that MAN1 shares a conserved globular domain of approximately 40 amino acids, which we term the LEM module, with inner nuclear membrane proteins lamina-associated polypeptide 2 and emerin. The LEM module is also present in two proteins of Caenorhabditis elegans. These results show that MAN1 is an integral protein of the inner nuclear membrane that shares the LEM module with other proteins of this subcellular localization.
منابع مشابه
LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins.
The LEM (lamina-associated polypeptide-emerin-MAN1) domain is a motif shared by a group of lamin-interacting proteins in the inner nuclear membrane (INM) and in the nucleoplasm. The LEM domain mediates binding to a DNA-crosslinking protein, barrier-to-autointegration factor (BAF). We describe a novel, ubiquitously expressed LEM domain protein, LEM2, which is structurally related to MAN1. LEM2 c...
متن کاملIntracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane.
MAN1 is an integral protein of the inner nuclear membrane that shares the LEM domain, a conserved globular domain of approximately 40 amino acids, with lamina-associated polypeptide (LAP) 2 and emerin. Confocal immuofluorescence microscopy studies of the intracellular targeting of truncated forms of MAN1 showed that the nucleoplasmic, N-terminal domain is necessary for inner nuclear membrane re...
متن کاملNuclear membrane protein MAN1: direct binding to emerin in vitro and two modes of binding to BAF
MAN1 is a vertebrate nuclear inner membrane protein that inhibits Smad signaling downstream of TGF . MAN1 has an exposed LEM-domain-containing Nterminal region (‘MAN1-N’), two transmembrane domains and an exposed Cterminal domain (‘MAN1-C’). Many regions of human MAN1 are homologous to emerin, a LEM-domain nuclear protein, loss of which causes Emery-Dreifuss muscular dystrophy (EDMD). To test t...
متن کاملEvolvement of LEM proteins as chromatin tethers at the nuclear periphery.
The nuclear envelope in eukaryotic cells has important roles in chromatin organization. The inner nuclear membrane contains over 60 transmembrane proteins. LEM [LAP2 (lamina-associated polypeptide 2)/emerin/MAN1] domain-containing proteins of the inner nuclear membrane are involved in tethering chromatin to the nuclear envelope and affect gene expression. They contain a common structural, bihel...
متن کاملThe endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo.
The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) defines a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF). Here, we describe a LEM protein annotated in databases as 'Ankyrin repeat and LEM domain-containing protein 1' (Ankle1). We show that Ankle1 is co...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 275 7 شماره
صفحات -
تاریخ انتشار 2000