Effects of the storage conditions on the stability of natural and synthetic cannabis in biological matrices for forensic toxicology analysis: An update from the literature
AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1gene.[5][6]
Function
Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two transcript variants encoding different isoforms have been found for this gene.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Peyrard M, Parveneh S, Lagercrantz S, Ekman M, Fransson I, Sahlén S, Dumanski JP (Jun 1998). "Cloning, expression pattern, and chromosomal assignment to 16q23 of the human gamma-adaptin gene (ADTG)". Genomics. 50 (2): 275–80. doi:10.1006/geno.1998.5289. PMID9653655.
^ abNogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S (Jul 2002). "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain". Nature Structural Biology. 9 (7): 527–31. doi:10.1038/nsb808. PMID12042876. S2CID42630285.
^Takatsu H, Yoshino K, Nakayama K (May 2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin". Biochemical and Biophysical Research Communications. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID10814529.
^Horikawa HP, Kneussel M, El Far O, Betz H (Nov 2002). "Interaction of synaptophysin with the AP-1 adaptor protein gamma-adaptin". Molecular and Cellular Neurosciences. 21 (3): 454–62. doi:10.1006/mcne.2002.1191. PMID12498786. S2CID54366866.
Further reading
Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Takatsu H, Yoshino K, Nakayama K (May 2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin". Biochemical and Biophysical Research Communications. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID10814529.
Takatsu H, Futatsumori M, Yoshino K, Yoshida Y, Shin HW, Nakayama K (Jun 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system". Biochemical and Biophysical Research Communications. 284 (4): 1083–9. doi:10.1006/bbrc.2001.5081. PMID11409905.
Shiba Y, Takatsu H, Shin HW, Nakayama K (Mar 2002). "Gamma-adaptin interacts directly with Rabaptin-5 through its ear domain". Journal of Biochemistry. 131 (3): 327–36. doi:10.1093/oxfordjournals.jbchem.a003107. PMID11872161.
Austin C, Boehm M, Tooze SA (Apr 2002). "Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry. 41 (14): 4669–77. doi:10.1021/bi016064j. PMID11926829.
Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S (Jul 2002). "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain". Nature Structural Biology. 9 (7): 527–31. doi:10.1038/nsb808. PMID12042876. S2CID42630285.