Dolichol phosphate in protein glycosylation In eukaryotic N-linked glycosylation, what is the functional role of dolichol phosphate within the endoplasmic reticulum membrane?

Introduction / Context:
Protein glycosylation is a major co-translational and post-translational modification affecting folding, stability, and trafficking. Understanding the lipid-linked oligosaccharide (LLO) pathway clarifies how glycans are built and transferred in the endoplasmic reticulum (ER).

Given Data / Assumptions:

• Focus on N-linked glycosylation (Asn-X-Ser/Thr motifs).
• Location: ER membrane.
• Key intermediate: dolichol phosphate (Dol-P), a long-chain polyisoprenoid lipid.

Concept / Approach:
In the LLO pathway, sugars are sequentially added to Dol-P on the cytosolic and luminal faces of the ER to assemble a defined oligosaccharide (typically Glc3Man9GlcNAc2). Oligosaccharyltransferase then transfers this glycan en bloc to an asparagine residue of the nascent polypeptide.

Step-by-Step Solution:
Identify Dol-P as a membrane-embedded polyisoprenoid phosphate.Understand that sugars (from nucleotide-sugar donors) are built onto Dol-P to form Dol-PP-oligosaccharide.Recognize the en bloc transfer by oligosaccharyltransferase to the acceptor asparagine.Conclude Dol-P functions as the lipid anchor for glycan assembly and delivery.

Verification / Alternative check:
Defects in dolichol or glycosylation enzymes cause congenital disorders of glycosylation, highlighting Dol-P’s essential role.

Why Other Options Are Wrong:

• Vesicle docking involves SNAREs and Rab GTPases, not dolichol.
• Chaperones like BiP/Calnexin assist folding; they are proteins, not lipids.
• Phospholipase C generates diacylglycerol and inositol phosphates, not dolichol derivatives.
• ATP transport into ER uses other mechanisms; Dol-P is not a transporter.

Common Pitfalls:
Confusing dolichol phosphate with phosphoinositide signaling lipids due to similar “phosphate” terminology.

Final Answer:
A lipid anchor on which an oligosaccharide assembles before transfer to nascent proteins