8.A.238. The Cell Permeabiity Peptide (CPP) Family Some members of this family directly, or indirectly, regulate GLUT2 gene expression and beta-cell function. They appear to play a role in cell signaling in mature and developing nerve terminals. They may also function as regulators of vesicle transport, through interactions with the JNK-signaling components and motor proteins. They function as anti-apoptotic proteins. Their levels seem to influence the beta-cell death or survival response (Harders et al. 2024).
References:
Akama, K.T., L.I. Thompson, T.A. Milner, and B.S. McEwen. (2013). Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled receptor 30 (GPR30), an estrogen receptor that can be identified in hippocampal dendritic spines. J. Biol. Chem. 288: 6438-6450.
Harders, R.H., T.H. Morthorst, L.E. Landgrebe, A.D. Lande, M.S. Fuglsang, S.B. Mortensen, V. Feteira-Montero, H.H. Jensen, J.B. Wesseltoft, and A. Olsen. (2024). CED-6/GULP and components of the clathrin-mediated endocytosis machinery act redundantly to correctly display CED-1 on the cell membrane in Caenorhabditis elegans. G3 (Bethesda) 14:.
Liu, Q.A. and M.O. Hengartner. (1999). Human CED-6 encodes a functional homologue of the Caenorhabditis elegans engulfment protein CED-6. Curr. Biol. 9: 1347-1350.
Noritake, J., Y. Fukata, T. Iwanaga, N. Hosomi, R. Tsutsumi, N. Matsuda, H. Tani, H. Iwanari, Y. Mochizuki, T. Kodama, Y. Matsuura, D.S. Bredt, T. Hamakubo, and M. Fukata. (2009). Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95. J. Cell Biol. 186: 147-160.
Smits, E., W. Van Criekinge, G. Plaetinck, and T. Bogaert. (1999). The human homologue of Caenorhabditis elegans CED-6 specifically promotes phagocytosis of apoptotic cells. Curr. Biol. 9: 1351-1354.
Examples:
TC#	Name	Organismal Type	Example
8.A.238.1.1	The C-Jun-terminal kinase-interacting protein, Jip1, 1 of 711 aas and possibly one N-terminal TMS. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response.		Jip1 of Homo sapiens

8.A.238.1.2	Mitogen-activated protein kinase 8 interacting protein 1. Jip1 of 474 aas		Jip1 of Mytilus edulis

8.A.238.1.3	CED6/GULF of 304 aas. It is a PTB domain-containing engulfment adapter protein 1 that functions as an adapter and is required for efficient phagocytosis of apoptotic cells. It modulates cellular glycosphingolipid and cholesterol transport, and may play a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP (Smits et al. 1999; Liu and Hengartner 1999). CED-6/GULP and components of the clathrin-mediated endocytosis machinery act redundantly to correctly display CED-1 on the cell membrane in Caenorhabditis elegans (Harders et al. 2024).		CED6/GULF of Homo sapiens