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Last update 08 May 2025

MAL2

Last update 08 May 2025

Basic Info

Synonyms

mal, T cell differentiation protein 2, MAL2, Protein MAL2

Introduction

Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway.

Drugs associated with MAL2

HG-1312

Target

MAL2

Mechanism

MAL2 modulators

Active Org.-

Originator Org.

Human Genome Sciences, Inc.

Active Indication-

Inactive Indication

Cardiovascular Diseases [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with MAL2

100 Translational Medicine associated with MAL2

0 Patents (Medical) associated with MAL2

157

Literatures (Medical) associated with MAL2

01 May 2025·Journal of Biological Chemistry

Maackia amurensis seed lectin structure and sequence comparison with other M. amurensis lectins

Article

Author: Nayak, Ashok R ; Temiakov, Dmitry ; Goldberg, Gary S ; Zhao, Caifeng ; Zheng, Haiyan ; Nicoletto, Rachel E ; Yin, Ariel C ; Holdcraft, Cayla J

Maackia amurensis lectins, including MASL, MAA, and MAL2, are widely utilized in biochemical and medicinal research. However, the structural and functional differences between these lectins have not been defined. Here, we present a high-resolution cryo-EM structure of MASL revealing that its tetrameric assembly is directed by two intersubunit disulfide bridges. These bridges, formed by C272 residues, are central to the dimer-of-dimers assembly of a MASL tetramer. This cryo-EM structure also identifies residues involved in stabilizing the dimer interface, multiple glycosylation sites, and calcium and manganese atoms in the sugar-binding pockets of MASL. Notably, our analysis reveals that Y250 in the carbohydrate-binding site of MASL adopts a flipped conformation, likely acting as a gatekeeper that obstructs access to non-cognate substrates, a feature that may contribute to MASL's substrate specificity. Sequence analysis suggests that MAA is a truncated version of MASL, while MAL2 represents a homologous isoform. Unlike MASL, neither MAL2 nor MAA contains a cysteine residue required for disulfide bridge formation. Accordingly, analysis of these proteins using reducing and nonreducing SDS-PAGE confirms that the C272 residue in MASL drives intermolecular disulfide bridge formation. These findings provide critical insights into the unique structural features of MASL that distinguish it from other Maackia amurensis lectins, offering a foundation for further exploration of its biological and therapeutic potential.

01 Apr 2025·Journal of Basic Microbiology

The Discovery of Novel ER‐Localized Cellobiose Transporters Involved in Cellulase Biosynthesis in Trichoderma reesei

Article

Author: Wu, Fu‐Gen ; Tu, Jing ; Huo, Liujie ; Wang, Haiyan ; Li, Chengcheng ; Shi, Xiaotong ; Lin, Fengming

ABSTRACTSugar transporters are of great importance in sensing and transporting varied sugars for cellulase biosynthesis of lignocellulolytic fungi. Nevertheless, the function and the relevant mechanism of sugar transporters in fungal cellulase biosynthesis remain to be explored. Here, putative maltose transporters Mal1, Mal2, Mal3, Mal4, and Mal5 in Trichoderma reesei were investigated. Despite that only the transcriptional abundance of Mal1 was upregulated under cellulase‐generating condition, the individual deletion of Mal1, Mal2, Mal3, Mal4, and Mal5 all impaired cellulase biosynthesis. The possible reason for this is that the individual knockout of Mal2, Mal3, Mal4, and Mal5 resulted in no gene expression of Mal1 at 24 h during the cellulase production. The transcriptional analysis showed that the absence of these transporters noticeably inhibited cellulase genes at 24 h, which was then relieved. Interestingly, the individual missing of these maltose transporters significantly retarded the cellular consumption of cellobiose, rather than maltose, and they were distributed in cytoplasm, largely in endoplasmic reticulum (ER). These findings manifested that these putative maltose transporters may be in fact endomembrane cellobiose transporters, influencing fungal cellulase generation probably through Mal1 at the early stage. This research advances the knowledge of endomembrane sugar transporters in fungal cellulase biosynthesis.

01 Mar 2025·Molecular Biology of the Cell

MAL2 and rab17 selectively redistribute invadopodia proteins to laterally-induced protrusions in hepatocellular carcinoma cells

Article

Author: Bassaro, Lauren. R. ; Davis, Saniya S. ; Tuma, Pamela L.

MAL2 (myelin and lymphocyte protein 2) and rab17 have been identified as hepatocellular carcinoma tumor suppressors. However, little is known how their functions in hepatic polarized protein sorting/trafficking translate into how they function in the epithelial-to-mesenchymal transition and/or the mesenchymal-to-epithelial transition in metastases. To investigate this, we expressed MAL2 and rab17 alone or together in hepatoma-derived Clone 9 cells (that lack endogenous MAL2 and rab17). Like MAL2, we found that rab17 expression led to the formation of actin- and cholesterol-dependent protrusions that correlated to its anti-oncogenic properties. MAL2 or rab17 selectively promoted the redistribution of invadopodia proteins to the protrusion tips that correlated with decreased matrix degradation. MAL2-mediated redistribution required a putative EVH1 recognition motif whereas rab17-mediated redistribution was GTP dependent. We also determined that MAL2 and rab17 interaction was GTP dependent, but not dependent on the MAL2 EVH1 recognition motifs, and that protrusions formed by their combined expression shared features of those induced by either alone. Finally, we report that MAL2 or rab17 can redirect trafficking of newly synthesized membrane proteins from the Golgi to the induced protrusions and that the EVH1 recognition motif was required in MAL2 and that rab17-mediated trafficking was GTP dependent.

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MAL2

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