A shortcut to the lysosome: The mannose-6-phosphate-independent pathway

Coutinho, Maria Francisca; Prata, Maria João; Alves, Sandra

doi:10.1016/j.ymgme.2012.07.012

Cited by 94 publications

(75 citation statements)

References 89 publications

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“…Its mammalian homolog, sortilin, plays a similar role and is apparently complementary to the mannose-6-phosphate lysosomal targeting pathway (53,54). The sortilin cytoplasmic tail binds to several cytosolic proteins that are necessary for its targeting function, including GGA and the AP3 complex (55).…”

Section: Discussionmentioning

confidence: 99%

SORCS1 is necessary for normal insulin secretory granule biogenesis in metabolically stressed β cells

Kebede¹,

Oler²,

Gregg³

et al. 2014

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

SORCS1 is necessary for normal insulin secretory granule biogenesis in metabolically stressed β cells

Kebede¹,

Oler²,

Gregg³

et al. 2014

J. Clin. Invest.

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“…However, it should be noted that MPR-independent pathways for TGN-to-endosome transport have also been described (Blanz et al, 2010;Coutinho et al, 2012). Indeed, studies on cells from patients with I-cell disease (a lysosomal storage disorder) have suggested the existence of an additional class of sorting receptors.…”

Section: Eesmentioning

confidence: 99%

“…Vps10p proteins are conserved throughout evolution from yeast to man, and in mammals they consist of five members: sortilin (also known as SORT1), SorCS1, SorCS2, SorCS3 and SorLA (also known as SORL1) (Coutinho et al, 2012;Willnow et al, 2008).…”

Section: Vps10p-domain-containing Receptorsmentioning

confidence: 99%

“…In the TGN, both sortilin and SorLA are able to bind to ligands, which include neurotensin and lysosomal proteins, such as acid sphingomyelinase and sphingolipid activator proteins (SAPs), as well as cathepsin D and cathepsin H, and mediate their transport to endosomes after recruitment of GGAs and AP-1 through their cytoplasmic tails (Canuel et al, 2008;Coutinho et al, 2012;Lefrancois et al, 2003;Nielsen et al, 2001). The ability of sortilin and SorLA to bind such a variety of diverse ligands explains why defects in their associated pathways are linked to different disorders that range from neurodegenerative to cardiovascular diseases (see Table 1).…”

Section: Vps10p-domain-containing Receptorsmentioning

confidence: 99%

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Bidirectional traffic between the Golgi and the endosomes – machineries and regulation

Progida

Bakke

2016

Journal of Cell Science

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The bidirectional transport between the Golgi complex and the endocytic pathway has to be finely regulated in order to ensure the proper delivery of newly synthetized lysosomal enzymes and the return of sorting receptors from degradative compartments. The high complexity of these routes has led to experimental difficulties in properly dissecting and separating the different pathways. As a consequence, several models have been proposed during the past decades. However, recent advances in our understanding of endosomal dynamics have helped to unify these different views. We provide here an overview of the current insights into the transport routes between Golgi and endosomes in mammalian cells. The focus of the Commentary is on the key molecules involved in the trafficking pathways between these intracellular compartments, such as Rab proteins and sorting receptors, and their regulation. A proper understanding of the bidirectional traffic between the Golgi complex and the endolysosomal system is of uttermost importance, as several studies have demonstrated that mutations in the factors involved in these transport pathways result in various pathologies, in particular lysosome-associated diseases and diverse neurological disorders, such as Alzheimer's and Parkinson's disease.

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“…Therefore, cathepsins are considered to be promising targets in anticancer therapy (Fricker, 2010). One possible mechanism by which cathepsins can be expressed at the cell membrane instead of intralysosomally, is via downregulation of molecular interactions with the insulin-like growth factor 2 receptor/ mannose-6-phosphate receptor (Coutinho et al, 2012). These receptors are responsible for transporting proteins into lysosomes.…”

Section: Cysteine Cathepsin Proteases and Its Small Molecular Inhibitorsmentioning

confidence: 99%

Potential Roles of Protease Inhibitors in Cancer Progression

Yang

Li³

2016

Asian Pacific Journal of Cancer Prevention

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Proteases are important molecules that are involved in many key physiological processes. Protease signaling pathways are strictly controlled, and disorders in protease activity can result in pathological changes such as cardiovascular and inflammatory diseases, cancer and neurological disorders. Many proteases have been associated with increasing tumor metastasis in various human cancers, suggesting important functional roles in the metastatic process because of their ability to degrade the extracellular matrix barrier. Proteases are also capable of cleaving non-extracellular matrix molecules. Inhibitors of proteases to some extent can reduce invasion and metastasis of cancer cells, and slow down cancer progression. In this review, we focus on the role of a few proteases and their inhibitors in tumors as a basis for cancer prognostication and therapy.

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A shortcut to the lysosome: The mannose-6-phosphate-independent pathway

Cited by 94 publications

References 89 publications

SORCS1 is necessary for normal insulin secretory granule biogenesis in metabolically stressed β cells

SORCS1 is necessary for normal insulin secretory granule biogenesis in metabolically stressed β cells

Bidirectional traffic between the Golgi and the endosomes – machineries and regulation

Potential Roles of Protease Inhibitors in Cancer Progression

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