Functional analysis of Slac2-c/MyRIP as a linker protein between melanosomes and myosin VIIa. (Q46520725)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15927964%20AND%20SRC:MED&resulttype=core&format=json

12 January 2020

title

Functional analysis of Slac2-c/MyRIP as a linker protein between melanosomes and myosin VIIa (English)

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12 January 2020

2

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12 January 2020

author name string

Taruho S Kuroda

series ordinal

1

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12 January 2020

language of work or name

English

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publication date

30 May 2005

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15927964%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

12 January 2020

number of pages

8

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based on heuristic

inferred from page(s)

published in

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12 January 2020

volume

280

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12 January 2020

issue

30

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12 January 2020

page(s)

28015-28022

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Rab proteins as membrane organizers

12 January 2020

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Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin

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Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport

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The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes

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A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport

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The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes

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Rab27A-binding protein Slp2-a is required for peripheral melanosome distribution and elongated cell shape in melanocytes.

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Melanosome transfer to and translocation in the keratinocyte

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Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene

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MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes

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