Research output: Contribution to journal › Review article › peer-review
Protein transport in plant cells. / Sharova, E. I.
In: Russian Journal of Plant Physiology, Vol. 49, No. 2, 01.12.2002, p. 255-268.Research output: Contribution to journal › Review article › peer-review
}
TY - JOUR
T1 - Protein transport in plant cells
AU - Sharova, E. I.
PY - 2002/12/1
Y1 - 2002/12/1
N2 - The subcellular localization and secretion of proteins synthesized in the cytosol are determined by short amino acid sequences in their molecules. N-terminal transit peptides provide for protein translocation across the membranes of the ER, mitochondria, plastids, and microbodies. Later, these peptides are cleaved off by processing peptidases. C-terminal peptides direct some proteins into microbodies and vacuoles. Transport into the nucleus and insertion in the membranes are determined by the specific sequences that reside in the molecule of the mature protein. Specific receptors associated with the protein-translocating channel recognize transit peptides. Protein unfolding is required for successful protein transport through these channels. Chaperones maintain proteins in such a state. Folded proteins cross the nuclear pore complex and the membrane of microbodies. Protein transport is tightly associated with their processing. During the vesicular protein transport within the endomembrane system (ER, Golgi apparatus, plasma membrane, and vacuoles), correct protein targeting is ensured by protein sorting during vesicle loading, the assembly of corresponding protein coats, vesicle transport to the acceptor membrane, and specific membrane fusion.
AB - The subcellular localization and secretion of proteins synthesized in the cytosol are determined by short amino acid sequences in their molecules. N-terminal transit peptides provide for protein translocation across the membranes of the ER, mitochondria, plastids, and microbodies. Later, these peptides are cleaved off by processing peptidases. C-terminal peptides direct some proteins into microbodies and vacuoles. Transport into the nucleus and insertion in the membranes are determined by the specific sequences that reside in the molecule of the mature protein. Specific receptors associated with the protein-translocating channel recognize transit peptides. Protein unfolding is required for successful protein transport through these channels. Chaperones maintain proteins in such a state. Folded proteins cross the nuclear pore complex and the membrane of microbodies. Protein transport is tightly associated with their processing. During the vesicular protein transport within the endomembrane system (ER, Golgi apparatus, plasma membrane, and vacuoles), correct protein targeting is ensured by protein sorting during vesicle loading, the assembly of corresponding protein coats, vesicle transport to the acceptor membrane, and specific membrane fusion.
KW - Chaperones
KW - Endoplasmic reticulum
KW - Golgi apparatus
KW - Microbodies
KW - Mitochondria
KW - Nucleus
KW - Plastids
KW - Protein transport
KW - Secretion
KW - Transit polypeptide
KW - Vacuoles
KW - Vesicles
UR - http://www.scopus.com/inward/record.url?scp=0036108821&partnerID=8YFLogxK
U2 - 10.1023/A:1014865910119
DO - 10.1023/A:1014865910119
M3 - Review article
AN - SCOPUS:0036108821
VL - 49
SP - 255
EP - 268
JO - Russian Journal of Plant Physiology
JF - Russian Journal of Plant Physiology
SN - 1021-4437
IS - 2
ER -
ID: 36420723