Target intelligence / Profile preview

Sad1 and UNC84 domain containing 1 (SUN1)

Target
SUN1
Molecular classification
Inner nuclear membrane protein, LINC complex component, Structural/Scaffolding protein (nucleocytoskeletal linker)
01

Overview

Sad1 and UNC84 domain containing 1 (SUN1) is a structural protein localized to the inner nuclear membrane, where it is a core component of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex[1][2][3][7]. SUN1 physically connects the nuclear lamina to the cytoskeleton, mediating nuclear positioning, movement, and the transmission of mechanical forces across the nuclear envelope[1][2][3]. It is essential for interkinetic nuclear migration in neuronal progenitors, the maturation of focal adhesions, actin cytoskeleton organization, and telomere attachment during meiosis[1][2]. Mutations in SUN1 have been associated with Emery-Dreifuss muscular dystrophy and rare developmental disorders, including neurological and muscular symptoms[1][2][4][5]. SUN1 is not a typical direct therapeutic target such as a receptor or enzyme, but its dysfunction is linked to various tissue pathologies due to deficits in nuclear-cytoskeletal communication[2][1][7].

Other names
SUN domain-containing protein 1KIAA0810UNC84AFLJ12407Protein unc-84 homolog ASad1/unc-84 protein-like 1Sad1 unc-84 domain protein 1sad1/unc-84 protein-like 1unc-84 homolog A
02

Biological functions

Nuclear anchorage and migrationMechanotransduction (mechanical signal transduction)Organization of actin cytoskeletonRegulation of intracellular traction forceMaturation of focal adhesionsTelomere attachment to the nuclear envelope during meiosisNucleokinesis and centrosome-nucleus coupling during neuronal and glial migrationmRNA export from the nucleus
03

Disease associations

Emery-Dreifuss muscular dystrophyMuscular dystrophyDevelopmental delay (case reports)(Potential involvement in other neurodevelopmental disorders)
04

Safety considerations

SUN1 deficiency may disrupt nuclear-cytoskeletal coupling, impair cell migration, and contribute to tissue pathologies[1][2].

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