Myelin proteolipid protein

Myelin proteolipid protein (PLP or lipophilin)

Identifiers

Symbol

Myelin_PLP

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Myelin proteolipid protein (PLP or lipophilin)^[1] is the major myelin protein from the central nervous system (CNS). It plays an important role in the formation or maintenance of the multilamellar structure of myelin. The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the efficiency of axonal impulse conduction.^[2]

In humans, point mutations in PLP are the cause of Pelizaeus–Merzbacher disease (PMD), a neurologic disorder of myelin metabolism. In animals demyelinating diseases such as mouse 'jimpy' or dog 'shaking pup' are also caused by mutations in PLP.

PLP is a highly conserved^[3] hydrophobic protein of 276 to 280 amino acids which seems to contain four transmembrane segments, two disulfide bonds and which covalently binds lipids (at least six palmitate groups in mammals).^[4] PLP is highly related to GPM6A, a neuronal membrane glycoprotein.^[5]

Human proteins containing this domain

GPM6A; GPM6B; PLP1;

References

^ Dautigny A, Popot JL, Pham Dinh D (1991). "Major Myelin proteolipid: the 4-alpha-helix topology". J. Membr. Biol. 120 (3): 233–246. doi:10.1007/BF01868534. PMID 1711121. S2CID 24450880.
^ Kitamura K, Sakamoto Y, Yoshimura K, Nishijima T, Uyemura K (1987). "Complete amino acid sequence of PO protein in bovine peripheral nerve myelin". J. Biol. Chem. 262 (9): 4208–4214. doi:10.1016/S0021-9258(18)61334-1. PMID 2435734.
^ Stoffel W, Schliess F (1991). "Evolution of the myelin integral membrane proteins of the central nervous system". Biol. Chem. Hoppe-Seyler. 372 (9): 865–874. doi:10.1515/bchm3.1991.372.2.865. PMID 1722981.
^ Weimbs T, Sto ffel W (1992). "Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP". Biochemistry. 31 (49): 12289–12296. doi:10.1021/bi00164a002. PMID 1281423.
^ Yan Y, Lagenaur C, Narayanan V (1993). "Molecular cloning of M6: identification of a PLP/DM20 gene family". Neuron. 11 (3): 423–431. doi:10.1016/0896-6273(93)90147-J. PMID 8398137. S2CID 46719251.

This article incorporates text from the public domain Pfam and InterPro: IPR001614

v t e Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)
Arrestin	SAG ARRB1 ARRB2 ARR3
Membrane-spanning 4A	MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18
Myelin	Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin-associated glycoprotein Myelin protein zero
Pulmonary surfactant	Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein C
Tetraspanin	TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34
Other/ungrouped	Calnexin LDL-receptor-related protein-associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF
see also other cell membrane protein disorders

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