Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha-actinin-1 is an F-actin cross-linking protein – a bundling protein that is thought to anchor actin to a number of intracellular structures.[6] Alpha-actinin-1 is a non-muscle cytoskeletal isoform found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.[7]
^Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (December 2000). "Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells". Blood. 96 (13): 4236–45. doi:10.1182/blood.V96.13.4236. PMID11110697.
^Feng S, Reséndiz JC, Christodoulides N, Lu X, Arboleda D, Berndt MC, Kroll MH (January 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry. 41 (4): 1100–8. doi:10.1021/bi0156005. PMID11802708.
Yürüker B, Niggli V (1992). "Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network". J. Cell Sci. 101 (2): 403–14. doi:10.1242/jcs.101.2.403. PMID1629252.
Tokuue Y, Goto S, Imamura M, et al. (1992). "Transfection of chicken skeletal muscle alpha-actinin cDNA into nonmuscle and myogenic cells: dimerization is not essential for alpha-actinin to bind to microfilaments". Exp. Cell Res. 197 (2): 158–67. doi:10.1016/0014-4827(91)90418-T. PMID1720388.
Nishiyama M, Ozturk M, Frohlich M, et al. (1990). "Expression of human alpha-actinin in human hepatocellular carcinoma". Cancer Res. 50 (19): 6291–4. PMID2169343.
Glück U, Ben-Ze'ev A (1995). "Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells". J. Cell Sci. 107 (7): 1773–82. doi:10.1242/jcs.107.7.1773. PMID7983147.
Maruyama K, Sugano S (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.
Egerton M, Moritz RL, Druker B, et al. (1996). "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes". Biochem. Biophys. Res. Commun. 224 (3): 666–74. doi:10.1006/bbrc.1996.1082. PMID8713105.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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.
Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
View the detailed Guide of Psilotum nudum: Detailed Study Of Psilotum Nudum (Whisk Fern), Classification, Anatomy, Reproduction
Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
View the detailed Guide of Psilotum nudum: Detailed Study Of Psilotum Nudum (Whisk Fern), Classification, Anatomy, Reproduction