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Association of Newly Synthesized Tubulin with Brain Microsomal Membranes
Author(s) -
Soifer David,
Czosnek Henryk
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb07868.x
Subject(s) - tubulin , membrane , microsome , association (psychology) , chemistry , neuroscience , biochemistry , biology , microbiology and biotechnology , psychology , microtubule , in vitro , psychotherapist
Abstract: Tubulin has been found to be synthesized on both membrane‐bound and free polyribosomes prepared from brain. Cell‐free studies indicate that tubulin made on rough microsomes is incorporated into the endoplasmic reticulum membrane as it is synthesized. This tubulin remains associated with the membrane after sedimentation and washing. The tubulin is not removed from the membrane after stripping ribosomes from the membranes in KCI‐puromycin, followed by repeated washing by either sedimentation or flotation in 0.5 M‐KCI. The membrane tubulin is partially susceptible to proteolysis by trypsin and chymotrypsin: /3‐tubulin is more accessible to the proteases than is a‐tubulin. Nonionic detergents extract mostly /3‐tubulin from the microsomal membrane. Newly synthesized tubulin which has been extracted from microsomal membranes in 0.5% Nonidet P‐40, coassembles and disassembles with carrier microtubule protein. The insertion of newly synthesized tubulin into endoplasmic reticulum membrane may be the first step in the incorporation of tubulin into the plasma membrane.