BERP, a Novel Ring Finger Protein, Binds to α-Actinin-4

El-Husseini, Alaa; Kwasnicka, Dorota A.; Yamada, Tesshi; Hirohashi, Setsuo; Vincent, Steven R.

doi:10.1006/bbrc.1999.2045

Cited by 39 publications

(34 citation statements)

References 32 publications

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“…We considered the existence of an hrs/actinin-4/BERP/ myosin V complex based on the binary interactions between hrs and actinin-4, actinin-4 and BERP (El-Husseini et al, 2000), and BERP with myosin V (El-Husseini and Vincent, 1999). BERP is a ring-finger containing protein that interacts with the tail domain of myosin V (El-Husseini and Vincent, 1999) through its C-terminal region and interacts with actinin-4 through its N-terminal region (El-Husseini et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…BERP is a ring-finger containing protein that interacts with the tail domain of myosin V (El-Husseini and Vincent, 1999) through its C-terminal region and interacts with actinin-4 through its N-terminal region (El-Husseini et al, 2000). BERP may function as an adapter protein between actinin-4 that has bound to endosomes and myosin V because it is enriched with endosomal membranes.…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, myosin Vb, a processive motor (Yildiz et al, 2003), is present on early endosomes and is involved in receptor recycling (Evans et al, 1997;Lapierre et al, 2001). Moreover, myosin V binds to BERP (El-Husseini and Vincent, 1999), a ring-finger protein of unknown function that also interacts with actinin-4 (El- Husseini et al, 2000). We reasoned that an hrs/actinin-4/BERP/myosin V protein complex could link sorting endosomes with the actin cytoskeleton and enable their motility for receptor recycling.…”

mentioning

confidence: 99%

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CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

Yan

Wei

Kujala

et al. 2005

MBoC

115

121

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Altering the number of surface receptors can rapidly modulate cellular responses to extracellular signals. Some receptors, like the transferrin receptor (TfR), are constitutively internalized and recycled to the plasma membrane. Other receptors, like the epidermal growth factor receptor (EGFR), are internalized after ligand binding and then ultimately degraded in the lysosome. Routing internalized receptors to different destinations suggests that distinct molecular mechanisms may direct their movement. Here, we report that the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling but not for EGFR degradation. The hrs/actinin-4/BERP/myosin V (CART [cytoskeleton-associated recycling or transport]) complex assembles in a linear manner and interrupting binding of any member to its neighbor produces an inhibition of transferrin recycling rate. Disrupting the CART complex results in shunting receptors to a slower recycling pathway that involves the recycling endosome. The novel CART complex may provide a molecular mechanism for the actin-dependence of rapid recycling of constitutively recycled plasma membrane receptors. INTRODUCTIONEndocytosis is required for the uptake of essential nutrients from the extracellular environment as well as for retrieval of proteins and lipids that are added to the plasma membrane during fusion of regulated and constitutive secretory vesicles (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). The endocytic pathway can be separated into numerous stages based on the movement of cargo and the identification of morphologically defined compartments (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). Early events in the endocytic process include membrane invagination and vesicle budding from the plasma membrane, formation of transport vesicles, and fusion with early endosomes. Later events include cargo sorting, and additional transport/fusion steps, including those responsible for transport to the lysosome for degradation, and those responsible for recycling back to various compartments (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). Although much progress has been made in elucidating the molecular processes involved in early endocytic events, such as those involved in the genesis of clathrin-coated endocytic transport vesicles, an equally clear understanding of later events remains elusive.The early endosome is a crucial point in the endocytic pathway to sort cargo for transport to late endosomes for eventual degradation in the...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

Yan

Wei

Kujala

et al. 2005

MBoC

115

121

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“…The mouse HAC1 is a novel protein with an unknown function. The rat BERP was cloned recently and was shown to interact with myosin V and aactinin-4 suggesting a role for BERP in myosin Vmediated cargo transport or in anchoring class V myosin to speci®c cell domains via its interaction with a-actinin-4 (El- Husseini and Vincent, 1999;El-Husseini et al, 2000). BERP shares 99% identity with the mouse HAC1.…”

Section: The Brat Gene Familymentioning

confidence: 99%

“…In rats, myosin V has a role in organelle transport along the axon and at the nerve terminal (Larson, 1996). The RING ®nger/B-box/ coiled-coil (RBCC) domain of BERP is required for BERP dimerization, and for binding with a-actinin-4, a non-muscle calcium-insensitive actinin (El-Husseini et al, 2000). Upon administration of nerve growth factor (NGF), PC12 cells normally start di erentiating; they stop dividing and develop neurite outgrowth.…”

Section: The Brat Protein Familymentioning

confidence: 99%

Mutations in the β-propeller domain of the Drosophila brain tumor (brat) protein induce neoplasm in the larval brain

et al. 2000

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Inactivation of both alleles of the fruit¯y D. melanogaster brain tumor (brat) gene results in the production of a tumor-like neoplasm in the larval brain, and lethality in the larval third instar and pupal stages. We cloned the brat gene from a transposon-tagged allele and identi®ed its gene product. brat encodes for an 1037 amino acid protein with an N-terminal B-box1 zinc ®nger followed by a B-box2 zinc ®nger, a coiled-coil domain, and a C-terminal b-propeller domain with six blades. All these motifs are known to mediate protein ± protein interactions. Sequence analysis of four brat alleles revealed that all of them are mutated at the bpropeller domain. The clustering of mutations in this domain strongly suggests that it has a crucial role in the normal function of Brat, and de®nes a novel protein motif involved in tumor suppression activity. The brat gene is expressed in the embryonic central and peripheral nervous systems including the embryonic brain. In third instar larva brat expression was detected in the larval central nervous system including the brain and the ventral ganglion, in two glands ± the ring gland and the salivary gland, and in parts of the foregut ± the gastric caecae and the proventriculus. A second brat-like gene was found in D. melanogaster, and homologs were identi®ed in the nematode, mouse, rat, and human. Accumulated data suggests that Brat may regulate proliferation and di erentiation by secretion/transportmediated processes.

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α‐Actinins

Takada

Beggs

2002

Wiley Encyclopedia of Molecular Medicine

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BERP, a Novel Ring Finger Protein, Binds to α-Actinin-4

Cited by 39 publications

References 32 publications

CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

Mutations in the β-propeller domain of the Drosophila brain tumor (brat) protein induce neoplasm in the larval brain

α‐Actinins

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