Disks large-associated protein 1 (DAP-1), also known as guanylate kinase-associated protein (GKAP), is a
protein that in humans is encoded by the DLGAP1gene. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the
post-synaptic density.[5]
Function
This gene encodes the protein called guanylate kinase-associated protein (GKAP). GKAP binds to the
SHANK2 and
PSD-95 proteins, facilitating the assembly of the post-synaptic density of neurons.[6] Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.
The interaction with PSD95 and S-SCAM is mediated by the GUK domain[13] and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.
^Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A (eds.). Molecular mechanisms of synaptogenesis. Berlin: Springer. pp. 72–75.
ISBN978-0-387-32560-6.
Suzuki T, Li W, Zhang JP, et al. (2005). "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins". Eur. J. Neurosci. 21 (2): 339–50.
doi:
10.1111/j.1460-9568.2005.03856.x.
PMID15673434.
S2CID28773407.
Disks large-associated protein 1 (DAP-1), also known as guanylate kinase-associated protein (GKAP), is a
protein that in humans is encoded by the DLGAP1gene. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the
post-synaptic density.[5]
Function
This gene encodes the protein called guanylate kinase-associated protein (GKAP). GKAP binds to the
SHANK2 and
PSD-95 proteins, facilitating the assembly of the post-synaptic density of neurons.[6] Dlgap1 has five 14-amino-acid repeats and three Pro-rich portions.
The interaction with PSD95 and S-SCAM is mediated by the GUK domain[13] and it has been hypothesized that this might mean it can also interact with other GUK containing proteins.
^Hines RM, El-Husseini A (2006). "Mechanisms that regulate neuronal protein clustering at the synapse". In El-Husseini A, Dityatev A (eds.). Molecular mechanisms of synaptogenesis. Berlin: Springer. pp. 72–75.
ISBN978-0-387-32560-6.
Suzuki T, Li W, Zhang JP, et al. (2005). "A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins". Eur. J. Neurosci. 21 (2): 339–50.
doi:
10.1111/j.1460-9568.2005.03856.x.
PMID15673434.
S2CID28773407.