Barrier-to-autointegration factor 1 (BANF1)

Barrier-to-autointegration factor 1 (BANF1) is a highly conserved, small, non-specific DNA-binding protein found in multicellular eukaryotes[1][2][3][4][5]. BANF1 functions as a homodimer, binding to the phosphate backbone of double-stranded DNA and compacting DNA, which helps maintain chromatin organization and genome stability[1][2][3]. It is a critical component of the nuclear envelope, essential for both the assembly and disassembly of the nuclear envelope during cell division[1][2]. BANF1 interacts with key nuclear envelope proteins, including Lamin A, Emerin, and other LEM-domain proteins, anchoring chromatin to the nuclear periphery and regulating nuclear structure[1][2][4]. Loss or mutation of BANF1 leads to loss of nuclear envelope integrity, aberrant chromatin organization, and is genetically linked to the rare premature ageing disorder Néstor–Guillermo Progeria Syndrome (NGPS)[1][2][6]. BANF1 also regulates the DNA repair protein PARP1 and is involved in the DNA damage response, especially in oxidative stress[1][6]. Besides its DNA structural role, BANF1 prevents inappropriate activation of innate immune sensors during nuclear envelope rupture by outcompeting DNA sensors such as cGAS for double-stranded DNA binding[1]. BANF1 is not a typical therapeutic target (i.e., not a receptor, enzyme, transporter, or transcription factor) but is a structural nuclear assembly factor with broad importance in genome maintenance.

Other names

BAFNGPSBCRP1D14S1460barrier-to-autointegration factorBAF nuclear assembly factor 1Breakpoint cluster region protein 1