POMK regulates dystroglycan function via LARGE-mediated elongation of matriglycan (Q99716328)

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29 September 2020

title

POMK regulates dystroglycan function via LARGE-mediated elongation of matriglycan (English)

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29 September 2020

7

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Junyu Xiao

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29 September 2020

Jack E. Dixon

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29 September 2020

Kevin P Campbell

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29 September 2020

author name string

Ameya S Walimbe

1

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29 September 2020

Hidehiko Okuma

2

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29 September 2020

Soumya Joseph

3

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29 September 2020

Tiandi Yang

4

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29 September 2020

Takahiro Yonekawa

5

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29 September 2020

Jeffrey M Hord

6

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29 September 2020

Mary E Anderson

8

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29 September 2020

Silvia Torelli

9

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29 September 2020

Adnan Manzur

10

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29 September 2020

Megan Devereaux

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29 September 2020

Marco Cuellar

12

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29 September 2020

Sally Prouty

13

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29 September 2020

Saul Ocampo Landa

14

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29 September 2020

Liping Yu

15

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29 September 2020

Francesco Muntoni

18

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29 September 2020

publication date

25 September 2020

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29 September 2020

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29 September 2020

volume

9

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SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function

29 September 2020

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Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE

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The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin

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O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

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Structural basis of laminin binding to the LARGE glycans on dystroglycan

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Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of alpha-dystroglycan

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Identifiers

DOI

10.7554/ELIFE.61388

1 reference

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29 September 2020

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