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FLASH GENE

Symbol

GABARAPL1

contributors: mct/np - updated : 30-08-2015

HGNC name	GABA(A) receptor-associated protein like 1
HGNC id	4068

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

PROTEIN

PHYSICAL PROPERTIES		basic
STRUCTURE

motifs/domains

N terminal tubulin binding motif

HOMOLOGY

interspecies	ortholog to murine Gabarapl1
	ortholog to murine Gabarapl2

intraspecies	homolog to GABARAP
	homolog to GABARAPL2
	homolog to GABARAPL3

Homologene

FAMILY

microtubule-associated protein (MAP) family, GABARAP subfamaily

CATEGORY

receptor

SUBCELLULAR LOCALIZATION	intracellular
	intracellular,cytoplasm,organelle,endoplasmic reticulum
	intracellular,cytoplasm,organelle,Golgi
	intracellular,cytoplasm,cytosolic,granule
	intracellular,cytoplasm,cytoskeleton,microtubule

basic FUNCTION	could participate in a complex clustering, targeting and/or degrading the GABA(A) receptors on post-synaptic membrane of neurons
	promoting tubulin assembly and microtubule bundling
	new member of the GABARAP family involved in the transport of GABA(A) receptor
	could participate in a complex clustering, targeting and/or degrading the GABA(A) receptors on post-synaptic membrane of neurons
	with its widespread distribution in the nervous system and its predominantly hydrophobic interactions, may have chaperone-like effects for many cell surface proteins along the biosynthesis pathway
	MAP1LC3A and MAP1LC3B and GABARAPs are essential for autophagosome formation and therefore suggest a dual role for individual members of this protein family
	displays a complex regulation that is different from that of other GABARAP family members
	tumor repressor inhibiting WNT signaling via mediating DVL2 degradation through the autophagy pathway
	GABARAPL1-interacting Rab GAPs are implicated in the reprogramming of the endocytic trafficking events under starvation-induced autophagy
	important role of ATG8 homologues may be to act as a scaffold for the assembly of autophagy complexes
	macroautophagic sequestration did not require the MAP1LC3 subfamily, but, intriguingly, GABARAP, GABARAPL1, GABARAPL2 are essential
	GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B, are not essential for autophagosome formation but are critical for autophagosome-lysosome fusion

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

INTERACTION

DNA

RNA

small molecule

protein	interacts with tubulin and GABA(A) receptor
	ATG4B displays increased activity against GABARAPL1
	interacting with STBD1, and AIM in STBD1 is responsible for its interaction with GABARAPL1
	HSP90AA1 interacts and protects GABARAPL1 from its degradation by the proteasome
	strong evidence that transcriptional repression plays a major role in regulating GARAPL1/MAP1LC3A levels, and this up-regulation results in an increase in the size of the autophagosome
	MAP1LC3B, GABARAP and GABARAPL1 are novel interactors of MAPK15, a MAP kinase involved in cell proliferation and transformation
	ULK1 interacted most strongly with GABARAP and GABARAPL1, but it also interacted with GABARAPL2, MAP1LC3A, and MAP1LC3C
	TBC1D5 controls cellular endomembrane trafficking processes and binds the retromer subunit VPS29 and the ubiquitin-like protein GABARAPL1
	GABARAP subfamily members, GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B, are primary contributors to PINK1/Parkin mitophagy and starvation autophagy
	FKBP8 is an GABARAPL1, GABARAPL2-interacting protein
	ATG4B, a key enzyme in autophagy that cleaves GABARAPL1, is an interactor of the small GTPase RAB7B
	ATG7 recognizes GABARAPL1, GARAPL2 through multiple steps, which would be necessary to induce a conformational change in ATG7 that is optimal for the activation reaction
	novel function of GABARAPL1 to activate TFEB, a master transcription factor of autophagy and lysosome function during lysosomal damage

cell & other

REGULATION

ASSOCIATED DISORDERS

ANIMAL & CELL MODELS