Abstract
Abstract: The L1‐ and F11‐like axonal glycoproteins, implicated in neurite outgrowth and fasciculation, are members of the Ig superfamily comprising multiple fibronectin type III‐like domains. Their Ig‐like and fibronectin type III‐related domains are likely to be composed of seven β‐strands arranged in two opposing β‐sheets of highly similar topology. Whereas the F11‐like molecules lack a transmembrane sequence and are anchored in the plasma membrane by a glycosylphosphatidylinositol, the L1 ‐like molecules comprise cytoplasmic domains with highly conserved sequence motifs. Most of the latter proteins occur in different isoforms generated by alternative pre‐mRNA splicing, which has not been documented for molecules of the F11 subgroup. L1 ‐like proteins undergo heterophils as well as homophilic interactions, whereas only the former mode of binding was observed for F11 ‐like proteins. Evidence is accumulating that these Ig superfamily molecules with fibronectin type III‐like domains are interacting in a complex manner with each other and molecules of the extracellular matrix. Investigations assigning structure to function reveal that their individual extracellular domains serve distinct binding activities. Recent studies also suggest that L1 and NCAM are implicated in the transduction of transmembrane signals.
References
138
Referenced
106
10.1016/0968-0004(92)90015-2
10.1146/annurev.bi.48.070179.004525
10.1073/pnas.84.2.600
10.1016/0896-6273(92)90197-L
10.1021/bi00122a025
10.1073/pnas.87.18.6934
10.1073/pnas.86.3.1088
10.1016/0092-8674(89)90029-9
10.1146/annurev.cb.07.110191.001001
10.1016/0962-8924(92)90183-N
/ Trends Cell Biol. / Interactions between GPI‐anchored proteins and membrane lipids by Brown D. A. (1992)10.1016/0896-6273(89)90073-1
{'key': 'e_1_2_2_13_1', 'first-page': '1', 'article-title': 'The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng‐CAM and restrictin', 'volume': '10', 'author': 'Brümmendorf T.', 'year': '1993', 'journal-title': 'Neuron'}
/ Neuron / The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng‐CAM and restrictin by Brümmendorf T. (1993)10.1083/jcb.112.5.1017
10.1016/0896-6273(91)90259-3
10.1083/jcb.108.4.1387
10.1083/jcb.118.5.1223
10.1002/jnr.490250205
10.1016/0896-6273(92)90023-7
10.1002/j.1460-2075.1985.tb02324.x
10.1016/0896-6273(89)90182-7
10.1126/science.3576199
10.1083/jcb.121.1.121
10.1016/S0076-6879(83)91049-2
10.1083/jcb.111.6.3087
10.1016/0092-8674(91)90548-D
10.1016/0092-8674(87)90178-4
10.1126/science.3055291
10.1016/0896-6273(88)90194-8
10.1016/0959-4388(92)90024-F
10.1016/0896-6273(90)90310-C
10.1016/0092-8674(91)90569-K
10.1038/356791a0
10.1016/0896-6273(92)90298-R
10.1146/annurev.bi.60.070191.001103
10.1016/0012-1606(92)90278-O
10.1016/0955-0674(91)90050-9
10.1523/JNEUROSCI.12-01-00257.1992
10.1146/annurev.bi.57.070188.001441
10.1002/bies.950140808
10.1042/bj2690321
10.1016/0006-291X(89)92724-1
10.1016/0092-8674(90)90223-2
10.1002/jnr.490330123
10.1083/jcb.109.2.775
10.1002/jnr.490310102
10.1083/jcb.98.5.1746
10.1083/jcb.106.2.487
10.1083/jcb.113.6.1399
10.1083/jcb.104.6.1579
10.1111/j.1432-1033.1990.tb15614.x
10.1146/annurev.cb.07.110191.002445
10.1016/0896-6273(90)90196-M
10.1038/320531a0
10.1101/SQB.1989.054.01.004
10.1016/0968-0004(90)90014-3
10.1083/jcb.110.1.193
10.1083/jcb.110.1.209
10.1083/jcb.118.5.1259
10.1002/j.1460-2075.1985.tb03847.x
10.1083/jcb.115.4.1113
10.1073/pnas.84.12.4337
10.1126/science.1279805
10.1016/0092-8674(85)90198-9
10.1523/JNEUROSCI.06-10-02987.1986
/ J. Neurosci. / The appearance of an LI‐like molecule in the chick primary visual pathway by Lemmon V. (1986)10.1016/0896-6273(89)90048-2
10.1242/dev.105.3.505
10.1016/S0959-437X(05)80183-2
10.1016/0968-0004(90)90195-H
10.1073/pnas.84.16.5615
10.1016/0304-4157(89)90014-2
10.1016/0092-8674(92)90600-H
10.1083/jcb.119.1.191
10.1073/pnas.84.7.2007
10.1016/0092-8674(89)90690-9
10.1016/0014-5793(91)80915-P
10.1038/334701a0
{'key': 'e_1_2_2_78_1', 'first-page': '59', 'article-title': 'Solubility and posttranslational regulation of GP130/F11—a neuronal GPI‐linked cell adhesion molecule enriched in the neuronal membrane skeleton', 'volume': '57', 'author': 'Moss D. J.', 'year': '1992', 'journal-title': 'Eur. J. Cell Biol.'}
/ Eur. J. Cell Biol. / Solubility and posttranslational regulation of GP130/F11—a neuronal GPI‐linked cell adhesion molecule enriched in the neuronal membrane skeleton by Moss D. J. (1992)10.1083/jcb.117.6.1311
10.1002/j.1460-2075.1988.tb03249.x
10.1016/0896-6273(92)90199-N
10.1002/j.1460-2075.1989.tb03563.x
/ EMBO J. / The cytoplasmic domain of the cell adhesion molecule uvomorulin associated with three independent proteins structurally related in different species by Ozawa M. (1990)10.1091/mbc.2.7.523
/ Cell Regul. / Identification of chicken embryo kinase 5, a developmentally regulated receptor‐type tyrosine kinase of the Eph family by Pasquale E. B. (1991)10.1523/JNEUROSCI.12-10-03956.1992
10.1083/jcb.111.6.2651
10.1016/0896-6273(93)90243-K
10.1038/309030a0
10.1006/dbio.1993.1081
10.1007/BF00214676
10.1242/dev.109.4.743
/ Development / A widely distributed antigen developmentally regulated in the nervous system by Pourquié O. (1990)10.1038/353076a0
10.1002/jnr.490300315
10.1083/jcb.107.4.1561
10.1083/jcb.118.4.937
10.1016/0955-0674(91)90119-J
10.1016/1044-5765(91)90047-R
10.1002/j.1460-2075.1984.tb01753.x
/ EMBO J. / Immunocytological and biochemical characterization of a new neuronal cell surface component (LI antigen) which is involved in cell adhesion by Rathjen F. G. (1984)10.1016/0092-8674(87)90107-3
10.1083/jcb.104.2.343
10.1242/dev.113.1.151
/ Development / Restrictin: a chick neural extracellular matrix protein involved in cell attachment co‐purifies with the cell recognition molecule F11 by Rathjen F. G. (1991)10.1016/S0021-9258(18)41808-X
10.1146/annurev.ne.14.030191.002531
10.1007/BF02919404
10.1091/mbc.1.8.567
/ Cell Regul. / Structural requirements for neural cell adhesion molecule‐heparin interaction by Reyes A. A. (1990)10.1016/0167-5699(91)90110-F
10.1083/jcb.109.5.2363
10.1016/0092-8674(84)90388-X
10.1038/348419a0
10.1083/jcb.104.4.957
10.1002/j.1460-2075.1989.tb03402.x
10.1016/0896-6273(89)90111-6
10.1126/science.2857501
10.1002/j.1460-2075.1990.tb07384.x
10.1002/cne.903100208
10.1021/bi00417a001
10.1083/jcb.119.6.1387
10.1002/jnr.490240203
10.1016/0092-8674(90)90805-O
10.1111/j.1432-1033.1989.tb14640.x
10.1126/science.2006419
10.1016/0896-6273(91)90366-8
10.1016/0968-0004(92)90491-Q
10.1016/0166-2236(91)90142-H
10.1002/jcb.240480110
10.1016/0092-8674(91)90063-5
10.1083/jcb.118.1.149
10.1016/1044-5765(91)90045-P
10.1242/dev.105.4.803
/ Development / Tissue specific O‐linked glycosylation of the neural cell adhesion molecule (N‐CAM) by Walsh F. S. (1989)10.1016/0166-2236(90)90097-T
10.1038/348411a0
10.1146/annurev.iy.06.040188.002121
10.1101/SQB.1989.054.01.075
10.1083/jcb.119.4.883
10.1111/j.1432-1033.1987.tb13453.x
10.1016/0006-291X(89)92688-0
10.1016/0092-8674(84)90188-0
10.1016/0092-8674(91)90062-4
10.1083/jcb.119.1.203
10.1111/j.1432-1033.1992.tb16655.x
Dates
Type | When |
---|---|
Created | 18 years, 8 months ago (Dec. 15, 2006, 9:15 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 24, 2023, 10:42 p.m.) |
Indexed | 3 months, 1 week ago (May 22, 2025, 5:48 a.m.) |
Issued | 31 years, 10 months ago (Oct. 1, 1993) |
Published | 31 years, 10 months ago (Oct. 1, 1993) |
Published Online | 18 years, 8 months ago (Dec. 15, 2006) |
Published Print | 31 years, 10 months ago (Oct. 1, 1993) |
@article{Br_mmendorf_1993, title={Axonal Glycoproteins with Immunoglobulin‐ and Fibronectin Type III‐Related Domains in Vertebrates: Structural Features, Binding Activities, and Signal Transduction}, volume={61}, ISSN={1471-4159}, url={http://dx.doi.org/10.1111/j.1471-4159.1993.tb13611.x}, DOI={10.1111/j.1471-4159.1993.tb13611.x}, number={4}, journal={Journal of Neurochemistry}, publisher={Wiley}, author={Brümmendorf, Thomas and Rathjen, Fritz G.}, year={1993}, month=oct, pages={1207–1219} }