Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 1 (ELFN1)

Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 1 (ELFN1) is a postsynaptic adhesion molecule predominantly expressed in the nervous system, notably in the cortex, hippocampus, and globus pallidus. ELFN1 contains an extracellular domain with six leucine-rich repeats (LRRs), a fibronectin type-III (FN3) domain, a transmembrane domain, and an extended intracellular segment. Functionally, ELFN1 plays an integral role at excitatory synapses onto certain interneurons, modulating the timing and probability of neurotransmitter release by organizing presynaptic group III metabotropic glutamate receptors (mGluRs) in a trans-synaptic manner, acting as an allosteric modulator of these receptors. ELFN1 also inhibits the activity of protein phosphatase 1 (PP1) complexes, directly impacting synaptic circuit dynamics and potentially overall neural plasticity. Mutations or dysregulation of ELFN1 have been implicated in neurological disorders such as Joubert syndrome 17 and other synaptopathies.

Other names

ELFN1Protein ELFN1PPP1R28Extracellular leucine-rich repeat and fibronectin type-III domain-containing protein 1Protein phosphatase 1 regulatory subunit 28Extracellular leucine-rich repeat and fibronectin type III containing 1

Allosteric modulation of group III metabotropic glutamate receptors (mGluR4, mGluR6, mGluR7, mGluR8); Synaptic adhesion and modulation of presynaptic neurotransmitter release probability; Inhibition of protein phosphatase 1 complexes