Protein targeting and modification are crucial processes that determine a protein's fate after synthesis. These mechanisms ensure proteins reach their intended destinations and acquire necessary modifications for proper function.
From signal sequences guiding proteins to specific cellular locations to post-translational modifications like glycosylation and phosphorylation, these processes fine-tune protein activity and interactions. Understanding these mechanisms is essential for grasping how cells regulate their protein machinery.
Protein Targeting
Signal Sequences and Recognition
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- Signal sequences consist of short amino acid sequences that direct proteins to specific cellular locations
- N-terminal signal sequences guide proteins to the endoplasmic reticulum (ER)
- Internal signal sequences direct proteins to mitochondria, chloroplasts, or peroxisomes
- Signal recognition particle (SRP) identifies and binds to signal sequences on nascent polypeptides
- SRP-ribosome complex docks with SRP receptor on ER membrane
- Nascent protein transfers to translocon for entry into ER lumen
Translocon Structure and Function
- Translocon forms a protein-conducting channel across ER membrane
- Consists of multiple protein subunits, including Sec61 complex
- Channel opens to allow polypeptide passage while maintaining membrane barrier
- Translocation can occur co-translationally or post-translationally
- Co-translational translocation involves ribosomes directly attached to translocon
- Post-translational translocation requires chaperone proteins to keep polypeptides unfolded
Protein Glycosylation
N-linked Glycosylation Process
- N-linked glycosylation attaches sugar chains to asparagine residues in proteins
- Occurs in the ER and Golgi apparatus
- Involves transfer of pre-assembled oligosaccharide to asparagine in Asn-X-Ser/Thr sequence
- Oligosaccharyltransferase catalyzes the initial attachment in the ER
- Further modifications occur in the Golgi apparatus
- N-linked glycans play roles in protein folding, stability, and cell-cell recognition
O-linked Glycosylation Mechanisms
- O-linked glycosylation attaches sugars to serine or threonine residues
- Primarily occurs in the Golgi apparatus
- Involves stepwise addition of individual monosaccharides
- No consensus sequence required for O-linked glycosylation
- O-linked glycans contribute to protein structure, stability, and signaling
- Mucins contain extensive O-linked glycosylation, important for their protective functions
Protein Modifications
Phosphorylation and Signaling
- Phosphorylation involves addition of phosphate groups to specific amino acids (serine, threonine, tyrosine)
- Catalyzed by protein kinases, reversed by protein phosphatases
- Regulates protein activity, interactions, and localization
- Plays crucial roles in signal transduction pathways
- Can activate or inhibit enzymes, creating molecular switches
- Phosphorylation cascades amplify and integrate cellular signals (MAP kinase pathways)
Ubiquitination and Protein Degradation
- Ubiquitination attaches ubiquitin molecules to lysine residues in target proteins
- Requires coordinated action of E1, E2, and E3 enzymes
- Polyubiquitination often targets proteins for degradation by the 26S proteasome
- Monoubiquitination can regulate protein localization or activity
- Ubiquitin-proteasome system maintains protein quality control and regulates cellular processes
- Deubiquitinating enzymes (DUBs) reverse ubiquitination, adding another layer of regulation
Proteolytic Processing and Activation
- Proteolytic processing involves cleavage of proteins by proteases
- Converts inactive precursor proteins (proproteins) into active forms
- Occurs in various cellular compartments and extracellular space
- Insulin production involves multiple proteolytic steps to generate active hormone
- Matrix metalloproteinases (MMPs) activate by proteolytic removal of propeptide domain
- Caspase activation in apoptosis relies on proteolytic processing cascade