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 -