Ribonucleoparticle-independent transport of proteins into mammalian microsomes.
There are at least two different mechanisms for the transport of secretory proteins into the mammalian endoplasmic reticulum. Both mechanisms depend on the presence of a signal peptide on the respective precursor protein and involve a signal peptide receptor on the cis-side and signal peptidase on the trans-side of the membrane. Furthermore, both mechanisms involve a membrane component with a cytoplasmically exposed sulfhydryl. The decisive feature of the precursor protein with respect to which of the two mechanisms is used is the chain length of the polypeptide. The critical size seems to be around 70 amino acid residues (including the signal peptide). The one mechanism is used by precursor proteins larger than about 70 amino acid residues and involves two cytosolic ribonucleoparticles and their receptors on the microsomal surface. The other one is used by small precursor proteins and relies on the mature part within the precursor molecule and a cytosolic ATPase.
Zimmermann
R
R
Institut für Physiologische Chemie, Universität München, Federal Republic of Germany.
Zimmermann
M
M
Wiech
H
H
Schlenstedt
G
G
Müller
G
G
Morel
F
F
Klappa
P
P
Jung
C
C
Cobet
W W
WW
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D004285:Dogs; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism*; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism*; D021382:Protein Sorting Signals; D012261:Ribonucleoproteins / Q000378:metabolism
D011498:Protein Precursors; D021382:Protein Sorting Signals; D012261:Ribonucleoproteins